Biochem Lab Endterm Notes

COLEGIO SAN AGUSTIN – BACOLOD BIOCHEMISTRY
College of Health and Allied Professions CHEM 2N

Nursing Program Lab Class
LECTURE NOTE
Emergence of Life
Life is nothing but thousands of ordered chemical reactions. In other words, chemistry is the logic of all biological
phenomena. By more or general consensus nowadays, an entity is considered to be "alive" if it has the capacity
to carry out three basic functional activities: metabolism, self-repair, and replication.
The emergence of life was quite a complex topic and various hypotheses were developed to try to describe how
life was formed. The prevailing hypotheses based on acquired promising evidences suggest that transition from
non-living to living entities was not a single event. The entire process is evolutionary and the process is
complex – starting from the simple organic compounds to intricate organic compounds that involved self-
replication, self-assembly, autocatalysis, and finally to the emergence of life.
Primordial Soup Hypothesis (Oparin-Haldane hypothesis)

In the 1920s, Alexander Oparin and J. B. S. Haldane independently proposed nearly identical hypotheses for how
life originated on Earth. Their hypothesis is now called the Oparin-Haldane hypothesis, and the key steps are:
1. formation of organic molecules, the building blocks of cells (e.g., amino acids, nucleotides, simple
sugars)
2. formation of polymers (longer chains) of organic molecules, that can function as enzymes to carry
out metabolic reactions, encode hereditary information, and possibly replicate (e.g., proteins, RNA
strands),
3. formation of protocells; concentrations of organic molecules and polymers that carry out metabolic
reactions within an enclosed system, separated from the environment by a semi-permeable
membrane, such as a lipid bilayer membrane
1. Formation of Organic Molecules

Oparin and Haldane posit the following assumptions of the condition of the early Earth that can support and
sustain the production of organic molecules.
1. The early Earth had a chemically reducing atmosphere.
2. This atmosphere, exposed to energy in various forms, produced simple organic building blocks
("monomers").
3. These compounds accumulated in a "soup" that may have concentrated at various locations (shorelines,
oceanic vents etc.).
4. By further transformation, more complex organic polymers—and ultimately life—developed in the
soup.
Palacios/Soliza
The primordial garnered esteemed support in the 1950s when Miller and Urey conducted a famous experiment.
The experiment aimed to simulate the environmental conditions of the Earth that led to the onset of creation of
organic compounds as elaborated by the hypothesis of Oparin and Haldane.
Miller – Urey Experiment
A gaseous chamber simulated an atmosphere with reducing compounds (electron donors) such as methane,
ammonia and hydrogen. Electrical sparks simulated lightning to provide energy. In only about a week’s time, this
simple apparatus caused chemical reactions that produced a variety of organic molecules, some of which are the
basic building blocks of life, such as amino acids. Although scientists no longer believe that pre-biotic Earth had
such a reducing atmosphere, such reducing environments may be found in deep-sea hydrothermal vents, which
also have a source of energy in the form of the heat from the vents. In addition, more recent experiments – that
used conditions that are thought to better reflect the conditions of early Earth – have also produced a variety of
organic molecules including amino acids and nucleotides - the building blocks of RNA and DNA (McCollom,
2013).
2011 reanalysis of the saved vials containing the original extracts that resulted from the Miller and Urey
experiments, using current and more advanced analytical equipment and technology, has uncovered more
biochemicals than originally discovered in the 1950s. One of the more important findings was 23 amino acids,
far more than the five originally found.
2. Formation of Organic Polymers
Because the process is continuous as the water cycle, organic molecules are accumulated over time. The high
concentration of these basic organic molecules form linkages that resulted to polymer (long chains of repeated
unit of an organic molecule (monomer)). The process is called polymerization.
• Amido acids + Amino Acids → Polypeptide Chains (Protein molecules)
Palacios/Soliza
• Ribose + Nitrogenous + Phosphate → nucleotide
nucleotides + nucleotides → nucleic acids (RNA and DNA)
3. formation of protocells
All life on Earth is composed of cells. Cells have lipid membranes that separate their inner contents, the
cytoplasm, from the environment. The lipid membranes allow cells to maintain high concentrations of
molecules like nucleotides needed for self-replicating RNAs to function more efficiently. Cells also
maintain large differences in concentration (concentration gradients) of ions across the membrane to drive
transport processes and cellular energy metabolism.
Lipids are hydrophobic, and will spontaneously self-assemble in water to form either micelles or lipid
bilayer vesicles. Vesicles that enclose self-replicating RNAs and other enzymes, take in reactants across the
membrane, export products, grow by accretion of lipid micelles, and divide by fission of the vesicle, are
called proto-cells and may have been the precursors of cellular life.
Palacios/Soliza
BIOCHEMISTRY
CHEM2N
lab class
Sensei Wilmark Palacios & Jhon Abrien Soliza
BIG
biology
biochemistry
chemistry
physics
SMALL
UNKNOWN
• Expansion of the Universe
Gravity becomes appreciable
Nebula
Birth of a
Star/Sun
Birth of the Solar
System
• Frequent Collision of massive
matters
Hadeon Era of
Earth
• Earth is being bombarded by
asteroids
Basic organic
molecules to
form
biomolecules
Primordial Soup
• Water condenses which nurtured life

Sources of Simple Organic Molecules
REDUCING ATMOSPHERE
HYDROTHERMAL VENTS
EXTRATERRESTRIAL
REDUCING ATMOSPHERE
MILLER – UREY EXPERIMENT
Methane
(CH4)
Hydrogen
(H2)
Ammonia
(NH3)
HYDROTHERMAL VENTS
Oxidizing Atmosphere
Reducing Atmosphere
EXTRATERRESTRIAL
Emergence of Life
Oparin – Haldane Hypothesis

(Primordial Soup Hypothesis)
STOICHIOMETRY – a balanced chemical
reaction
Number of Atoms are balanced.

REACTION and STOICHIOMETRIC RATIO:
H H Cl Cl H Cl
H Cl
1 PARTICLE 1 PARTICLE
2 PARTICLES
𝐻! + 𝐶𝑙! → 2𝐻𝐶𝑙
REACTION and STOICHIOMETRIC RATIO:
Fe 𝑁𝑂! Na Na 𝑁𝑂! Fe
1 PARTICLE 1 PARTICLE 1 PARTICLE 1 PARTICLE

The Mole
Fe 𝑁𝑂! Na Na 𝑁𝑂! Fe
1 PARTICLE 1 PARTICLE 1 PARTICLE 1 PARTICLE
1 mole 1 mole 1 mole 1 mole
Mole = 6. 022 x 10 ^ 23 particles

Chemical Reaction in Actual:
Molar Mass (g/mol) – converts mass of a compound to the total number of
particles (moles); and vice versa.
Stoichiometric Equation – converts the moles of one compound to another

compound according to their relative amounts in a chemical reaction
Example 1: How many moles does 5 g of 𝐶! 𝐻"# have?
Molar mass = g/mol

C= 12.01g/mol x 4 = 48.04g/mol
H= 1.008g/mol x 10 = 10.08g/mol
58.12g/mol C4H10
"#$%C4H10
5g C4H10 x = 0.09moles
58.12g
Example 2:
𝑍𝑛𝑆𝑂' + 2𝑁𝑎 → 𝑁𝑎 ( 𝑆𝑂' + 𝑍𝑛

"#$% &'()*
20g ZnSO4 = 0.124mol ZnSO4
"+".**-
1mol ZnSO4 / 2 mol Na mole ratio base on chem eq’n
.#$% /0
0.124mol ZnSO4 x = 0.248mol Na
1mol ZnSO4
.!-
0.248mol Na x "#$% /0 = 5.7g Na
"#$% &'()* .#$% /0 .!- /0

20g ZnSO4 x x = 5.7g Na
ZnSO4 20 g Na g? "+".**- 1mol ZnSO4 "#$% /0
Zn 65.38 g/mol + S
32.06g/mol + Na 23g/mol
(16g/mol O x 4)
161.44g/mol ZnSO4
Solution:
𝑆𝑜𝑙𝑢𝑡𝑖𝑜𝑛 = 𝑆𝑜𝑙𝑢𝑡𝑒 + 𝑆𝑜𝑙𝑣𝑒𝑛𝑡

70% ethanol 100mL
contains 70mL ethanol
solute 30ml is water
solvent
Solution
Expression of Concentration:
#011 1$%234
1. % 𝑏𝑦 𝑚𝑎𝑠𝑠 = ∗ 100% unit: %
#011 1$%235$'
#011 $6 1$%234
• 𝑝𝑝𝑡 (𝑝𝑎𝑟𝑡𝑠 𝑝𝑒𝑟 𝑡ℎ𝑜𝑢𝑠𝑎𝑛𝑑) = #011 1$%235$'
∗ 1000 unit: ppt
#011 $6 1$%234
• 𝑝𝑝𝑡 𝑝𝑎𝑟𝑡𝑠 𝑝𝑒𝑟 𝑚𝑖𝑙𝑙𝑖𝑜𝑛 = ∗ 1,000,000 unit: ppm
#011 1$%235$'
#011 $6 1$%234
• 𝑝𝑝𝑏 𝑝𝑎𝑟𝑡𝑠 𝑝𝑒𝑟 𝑏𝑖𝑙𝑙𝑖𝑜𝑛 = ∗ 1,000,000,000 unit: ppb
#011 1$%235$'
Units should be the same to cancel out
7$%2#4 1$%234
2. % 𝑏𝑦 𝑣𝑜𝑙𝑢𝑚𝑒 = ∗ 100% unit: %
7$%2#4 1$%235$' 5' 8
#$%41 1$%234
3. 𝑀𝑜𝑙𝑎𝑟𝑖𝑡𝑦 = ∗ 100% unit: moles/L or M
7$%2#4 1$%235$'
#$%41 1$%234
4. 𝑀𝑜𝑙𝑎𝑙𝑖𝑡𝑦 = ∗ 100% unit: moles/Kg or m
#011 1$%74'3 5' 9-
Molality example
Given: 85g NaOH and 1Kg water
Given: 500mL water, density of water 1g/mL,
0.75mol NaOH
Stoichiometric Calculations
The coefficients in the balanced equation give

the ratio of moles of reactants and products.
Stoichiometry
© 2012 Pearson Education, Inc.

Concentration of solutions
• The concentration of a solution is a
measure of the amount of solute that
has been dissolved in a given amount of
solvent or solution.
Stoichiometry
Percent Concentration
• Mass Percent (m/m)
Suppose that a solution was prepared by

dissolving 25.0g of sugar into 100g of water. The percent
by mass would be calculated as follows:
Stoichiometry

• Volume Percent (v/v)
If a solution is made by taking 40mL of ethanol and

adding enough water to make 240mL of solution, the
percent by volume is:
Stoichiometry

• Mass-volume concentration (m/v)
if a solution is prepared from 10g NaCl in enough water

to make a 150mL solution, the mass-volume
concentration is?
Stoichiometry

Molarity
• Two solutions can contain the same
compounds but be quite different because the
proportions of those compounds are different.
• Molarity is one way to measure the
concentration of a solution:
moles of solute
Molarity (M) =
volume of solution in liters
Stoichiometry

Mixing a Solution
• To create a solution of a
known molarity, one
weighs out a known mass
(and, therefore, number of
moles) of the solute.
• The solute is added to a
volumetric flask, and
solvent is added to the line
on the neck of the flask.
Stoichiometry

Dilution
The molarity of the new solution can be determined
from the equation
M1 ´ V1 = M2 ´ V2, C1 V1 = C2V2
where M1 and M2 are the molarity of the concentrated
and dilute solutions, respectively, and V1 and V2 are
the volumes of the two solutions.
Stoichiometry

Sample Exercise 4.11 Calculating Molarity
Calculate the molarity of a solution made by dissolving 23.4 g of sodium sulfate (Na2SO4) in enough water to form
125 mL of solution.
Solution
Analyze We are given the number of grams of solute Plan We can calculate molarity using Equation 4.32. To
(23.4 g), its chemical formula (Na2SO4), and the volume do so, we must convert the number of grams of solute to
of the solution (125 mL) and asked to calculate the moles and the volume of the solution from milliliters to
molarity of the solution. liters.
Solve The number of moles of Na2SO4 is obtained by

using its molar mass:
Converting the volume of the solution to liters:
Thus, the molarity is
Stoichiometry
Sample Exercise 4.11 Calculating Molarity
Continued
Practice Exercise
Stoichiometry
Sample Exercise 4.13 Using Molarity to Calculate Grams of Solute
How many grams of Na2SO4 are required to make 0.350 L of 0.500 M Na2SO4?
Solution
Stoichiometry
Sample Exercise 4.14 Preparing a Solution by Dilution
How many milliliters of 3.0 M H2SO4 are needed to? make 450 mL of 0.10 M H2SO4
Solution
Stoichiometry
Titration and Buffer Solution
(CHEM2N)
Jhon Abrien S. Soliza

Buffers
• A buffer can resist pH changes if the pH is at
or near a weak acid pKa value.
• Buffer range: the pH range where maximum

resistance to pH change occurs when adding
acid or base. It is = +1 pH from the weak acid
pKa
• If pK is 4.8 the buffering range is 3.8-5.8
• Buffer capacity: the molar amount of acid

which the buffer can handle without significant
changes in pH.
Buffers
If a small amount of hydroxide is added to an equimolar

solution of HF in NaF, for example, the
HF reacts with the OH- to make F- and water.
Buffers
Similarly, if acid is added, the F- reacts with it to form HF

and water.

Three major buffer systems of our body
• Extracellular Fluids
• ECFs are similar except for the
high protein content of plasma
• Sodium (Na+) is the major
cation
• Chloride (Cl-)is the major anion
• Intracellular Fluids
• Have low sodium and chloride
• Potassium (K+) is the chief cation
• Phosphate (PO4-) is the chief
anion
Buffer system in our body
Buffer Calculations
Consider the equilibrium constant expression for
the dissociation of a generic acid, HA:
HA + H2O H3O+ + A-
[H3O+] [A-]
Ka =
[HA]

Henderson - Hasselbalch equation
+ -
From [ H ][ A ]
K=
[ HA]
Rearrange + [ HA]
[H ] = K -
[A ]
Take (-)Log of each [ A- ]
pH = - log K + log
[ HA]
-
[A ]
pH = pK + log
[ HA]
Henderson–Hasselbalch Equation
What is the pH of a buffer that is 0.12 M in
lactic acid, CH3CH(OH)COOH, and 0.10 M in
sodium lactate? Ka for lactic acid is 1.4 ´ 10-4.
[A-]
pH = pKa + log
[HA]
pKa = 3.854
[0.1M]
pH = 3.854 + log
[0.12M]
pH= 3.77 Aqueous
Equilibria
Addition of Strong Acid or Base
to a Buffer
1. Determine how the neutralization
reaction affects the amounts of
the weak acid and its conjugate
base in solution.
2. Use the Henderson–Hasselbalch
equation to determine the new
pH of the solution.
Aqueous
Equilibria
Practice Exercise
Calculate the pH of a buffer composed of 0.12 M benzoic
acid and 0.20 M sodium benzoate. Ka 6.3x 10-5
Answer: 4.42
pKa= -log(Ka) =4.2
[0.2M]
pH = 4.2 + log
[0.12M]
Aqueous
Equilibria
Sample Exercise 17.4 Preparing a Buffer
How many moles of NH4Cl must be added to 2.0 L of 0.10 M NH3 to form a buffer whose pH is 9.00?
(Assume that the addition of NH4Cl does not change the volume of the solution.)
pOH = 14.00 – pH = 14.00 – 9.00 = 5.00 !"# (%"&) !"(

[OH–] = 1.0 ´ 10-5 M (Kb = (!"()
)%"&
[NH3] = 0.10 M
(2.0 L)(0.18 mol NH4CI/L) = 0.36 mol NH4CI
Aqueous
Equilibria
Sample Exercise 17.5 Calculating pH Changes in Buffers
A buffer is made by adding 0.300 mol CH3COOH and 0.300 mol CH3COONa to enough water to make
1.000 L of solution. The pH of the buffer is 4.74 (Sample Exercise 17.1).
(a) Calculate the pH of this solution after 5.0 mL of 4.0 M NaOH(aq) solution is added.
(b) For comparison, calculate the pH of a solution made by adding 5.0 mL of 4.0 M NaOH(aq) solution to 1.000 L of pure water.
Molarity
after
addition
1L+ 0.005L = 1.005L=V FINAL
Aqueous
Equilibria
Sample Exercise 17.5 Calculating pH Changes in Buffers
Continued
(b) To determine the pH of a solution made by adding 0.020 mol of NaOH to 1.000 L of pure water,
we first determine the concentration of OH– ions in solution,
[OH–] = 0.020 mol/(1.005 L) = 0.020 M
We use this value in Equation 16.18 to calculate pOH and then use our
calculated pOH value in Equation 16.20 to obtain pH:
pOH = –log[OH–] = –log(0.020) = +1.70
pH = 14 – (+1.70) = 12.30
Comment Note that the small amount of added NaOH changes the pH of
water significantly. In contrast, the pH of the buffer changes very little
when the NaOH is added, as summarized in Figure 17.4.
Aqueous
Equilibria
Titration
In this technique, a
known concentration of
base (or acid) is slowly
added to a solution of
acid (or base).
Aqueous
Equilibria
Key Terms
• Titration – A process where a solution of known strength is added to a
certain volume of a treated sample containing an indicator.
• Titrant – A solution of known strength of concentration used in the titration.
• Titrand – The titrand is any solution to which the titrant is added and which
contains the ion or species being determined.
• Titration curve – A plot of pH Vs milliliters of titrant showing the manner in
which pH changes Vs milliliters of titrant during an acid-base titration.
• Equivalence point – The point at which just adequate reagent is added to
react completely with a substance.
• Buffer solution – A solution that resists changes in pH even when a strong
acid or base is added or when it is diluted with water.
Aqueous
Equilibria
Titration
A pH meter or indicators are used to

determine when the solution has reached
the equivalence point, at which the
stoichiometric amount of acid equals
that of base. Aqueous
Equilibria
Types of Acid-Base Titration
Types Of Example
Titration
Strong acid-strong Hydrochloric acid
base and sodium
hydroxide
Weak acid-strong Ethanoic acid and

base sodium hydroxide
Strong acid-weak Hydrochloric acid

base and ammonia
Weak acid-weak Ethanoic and Aqueous

Equilibria
base ammonia
Choice of Indicators
Types Of Example
Titration
Strong acid- Phenolphthalein is usually preferred
strong base because of its more easily seen
colour change.
Weak acid-strong Phenolphthalein is used and change
base sharply at the equivalence point and
would be a good choice.
Strong acid-weak Methyl orange will change sharply at

base the equivalence point.
Weak acid-weak Neither phenolphthalein, not methyl

base orange is suitable. No indicator is
suitable because it requires a
vertical portion of the curve over two
pH units. Aqueous
Equilibria
Changes in pH during the titration of a strong acid
with a strong base
GIVEN: 50mL of 0.05M HCl vs 0.1M NaOH sol’n
Volume of NaOH, mL 0.1M Change in pH
NaOH
0.00
10.00
20.00
24.00
24.90
25.00
25.10
26.00
30.00
Aqueous
Equilibria
Aqueous
Equilibria
Aqueous
Equilibria
Aqueous
Equilibria
Aqueous
Equilibria
Aqueous
Equilibria
Sample Exercise 17.6 Calculating pH for a Strong Acid–Strong
Base Titration
Calculate the pH when (a) 49.0 mL and (b) 51.0 mL of 0.100 M NaOH
solution have been added to 50.0 mL
of 0.100 M HCl solution.
Vfinal = 50.0 mL + 49.0 mL = 99.0 mL = 0.0990 L
pH = –log(1.0 ´ 10-3) = 3.00
Aqueous
Equilibria
Sample Exercise 17.6 Calculating pH for a Strong Acid–Strong
Base Titration
(b) 51.0 mL of 0.100 M NaOH solution have

been added to 50.0 mL
of 0.100 M HCl solution.
pOH= 3
Vfinal = 50.0 mL + 51.0 mL = 101.0 mL = 0.1010 L (OH-)=10^-3
= 1 X 10^-3 M
pOH = –log(1.0 ´ 10-3) = 3.00 )*

51mL)+++,* =
pH = 14.00 – pOH = 14.00 – 3.00 = 11.00 0.051𝐿𝑠𝑜𝑙 - 𝑛
(0.1mol/1L sol’n)0.051L
Aqueous
sol’n= 5.1x 10-3mol OH- Equilibria
LIPIDS are heterogeneous class of naturally occurring bioorganic compounds that have the common
property of being soluble in non-polar solvents. They are grouped together not by the presence of a
distinguishing functional group or structural feature, but rather on the basis of common solubility properties:
*
they are insoluble in water but highly soluble in one or more organic solvents.
*
- although certain lipids contain ionized groups (e.g., phosphate or choline), the bulk of any lipid
molecule is nonpolar
- widely distributed in biological world and play a wide variety of roles in both plant and animal tissues:
o as an energy source, lipids provide 9 kcal of energy per gram
o triglycerides provide energy storage in adipocytes
o phosphoglycerides, sphingolipids, and steroids are structural components of cell membranes
o steroid hormones are critical intercellular messengers
o lipid-soluble vitamins (A, E, D, K)
o dietary fat acts as a carrier of lipid-soluble vitamins into cells of small intestine
o provide shock absorption and insulation
- the primary form of energy storage; stored fat allows certain animals to hibernate during winter
- has a very high energy value, twice as much as an equal weight of carbohydrates
- the amount of fat in the body is very much related to the carbohydrate level in the body: when
carbohydrate levels become low, fats are degraded to provide energy; when high, fats are stored
in cells of adipose tissues (under the skin, around the kidneys, etc.)
- structurally, the lipids are quite diverse; there is no common subunit in their structure.
- the primary building blocks in human lipids are fatty acids, glycerol, sphingosine, and sterols.
CLASSIFICATION OF LIPIDS
3.1 Fatty Acids 3.4 Complex lipids
3.2 Glycerides 3.4.1 Phospholipids
3.2.1 Neutral glycerides (TAG) 3.4.2 Glycolipids
3.2.2 Phosphoglycerides (lecithins, cephalins) 3.4.3 Lipoproteins
3.3 Nonglycerides 3.5 Miscellaneous Lipids
3.3.1 Waxes 3.5.1 Terpenes (carotenes)
3.3.2 Sphingolipids 3.5.2 Fat-soluble vitamins
a. sphingomyelin
b. glycolipid (cerebrosides)
c. ganglioside
3.3.3 Steroids
a. sterols c. sex hormones
b. bile acids/bile salts d. adrenocortical hormones
Classification of lipids on the basis of polarity and type of structural subunits present
A. Nonpolar, fatty-acid containing lipids (TAG: fats, oils)
B. Polar, fatty-acid containing lipids
a) Phosphoacylglycerols (lecithins, cephalins)
b) Sphingolipids (sphingomyelins, cerebrosides)
C. Non-fatty-acid containing lipids
Steroids: cholesterol, bile salts, steroid hormones (sex hormones, adrenocortical hormones)
3.1 FATTY ACIDS

- are long straight-chain (no branching) naturally occurring monocarboxylic acids; rarely found free in nature
but mostly in esterified form in the lipids
- as a consequence of their biosynthesis, fatty acids typically have an even # of C atoms, long-chain fa’s (12 -
26 C) are found in meats and fish; medium-chain (6 - 10 C) & short-chain fa’s (< 6C) primarily in dairy
products
- can be either saturated or unsaturated; saturated fatty acids have no double bonds, unsaturated fatty
th
acids contain one or more carbon-carbon double bonds, the first is usually at the 9 carbon
1
- the double bonds are not conjugated and are usually in a cis configuration; cis double bonds result in a
bent chain which doesn’t allow fatty acids to pack as close together and consequently lower the melting
point
H H O
C C CH2 CH2 CH2 C
O
CH2 CH2 CH2 CH2 CH2
CH2
CH2
CH2
CH2
CH3
saturated fatty acids (CnH2n + 1):

4:0 butyric acid n-butanoic C3H7COOH butter
6:0 caproic n-hexanoic C5H11COOH goat’s milk
8:0 caprylic n-octanoic C7H15COOH
10:0 capric n-decanoic C9H19COOH
12:0 lauric n-dodecanoic C11H23COOH coconut
14:0 myristic n-tetradecanoic C13H27COOH nutmeg
16:0 palmitic n-hexadecanoic C15H31COOH palm
18:0 stearic n-octadecanoic C17H35COOH animal fat
20:0 arachidic n-eicosanoic C19H39COOH peanut oil
unsaturated fatty acids : (up to six double bonds are found in biochemically important fatty acids)
∆9
16:1 palmitoleic cis-9-hexadecenoic acid C15H29COOH
∆9
18:1 oleic cis-9-octadecenoic C17H33COOH olive, corn
∆9,12
18:2 linoleic cis,cis-9,12-octadecadienoic C17H31COOH soybean,
safflower, sunflower
∆9,12,15
18:3 linolenic all cis-9,12,15-octadecatrienoic C17H29COOH herring, linseed
∆5,8,11,14
20:4 arachidonic all cis-5,8,11,14-eicosatetraenoic C19H31COOH
∆5,8,11,14,17
20:5 EPA
∆4,7,10,13,16,19
22:6 DHA
essential fatty acid is a PUFA that is needed by the human body and that must be obtained from dietary
sources because it cannot be synthesized within the body from other substances. Linoleic and linolenic acids
are called essential fatty acids that must be supplied in the diet.
omega (ω) fatty acids

- a fatty acid has two ends, the methyl (CH3) end and the carboxyl (COOH) end; the omega classification
system for fatty acid is based on numbering the carbon chain beginning at the methyl end, thus omega-3(ω3)
fatty acid is a PUFA with its endmost double bond three carbons away from its methyl end; omega-6 (ω6) fatty
acid is a PUFA with its endmost double bond six carbons away from its methyl end.
2
- Linolenic acid is the primary member of the ω3 family of fatty acids. From dietary linolenic acid, the body can
make the 20- and 22- carbon members of the ω3 fatty acid series. Omega-3 fatty acids are important for
the structure and function of cell membranes, particularly in the retina of the eye and the CNS. Because
fish are a good ω3 fatty acid source, nutritionists recommend adding more fish to the diet; cold-water fish
tend to have higher ω3fatty acid concentrations than do warm-water fish.
- Linoleic acid is the primary member of the ω6 family of fatty acids. Given dietary linoleic acid, the body can
make necessary longer carbon-chain members of the ω6 fatty acid series such as arachidonic acid (20:4).
Normally, vegetable oils and meats supply enough linoleic acid to meet the body’s needs for it. Omega-6
fatty acids are important for growth, skin integrity, fertility, and maintaining red blood cell structure. Lack
of linoleic acid causes the skin to redden and become irritated. Infants have especial need for linoleic acid
for their growth. Human breast milk has a much higher percentage of it then cow’s milk.
- Arachidonic acid, a 20:4 fatty acid, is an ω6 fatty acid synthesized from linoleic acid. In the body, it serves as the
precursor for a family of molecules called eicosanoids, which are oxygenated derivatives of this acid.
Eicosanoids are present in all cells except the red blood cells. Eicosanoids regulate a wide range of body
functions including blood pressure, blood clotting, blood lipid levels, the sleep/wake cycle, and the
inflammation response to injury and infection
- Eicosanoids are hormone-like molecules; they are not transported in the bloodstream to their site of action but
rather exert their effects in the tissues where they are synthesized. The name eikosanoid is derived from
the Greek word eikos, meaning twenty, because they are all derivatives of 20 carbon fatty acids. The
eicosanoids include three groups of structurally related compounds: the prostaglandins, the leukotrienes,
and the thromboxanes
3
Biological processes regulated by eicosanoids
1. Blood clotting - Thromboxane A2 stimulates constriction of blood vessels and platelet aggregation;
Prostacyclin dilates blood vessels and inhibits platelet aggregation
2. Inflammatory response - Prostaglandins mediate aspects of inflammatory response
3. Reproductive system - Stimulation of smooth muscle by PGE2
4. Gastrointestinal tract - Prostaglandins inhibit gastric secretion; Prostaglandins increase
secretion of protective mucus; Inhibition of hormone-sensitive lipases
5. Kidneys - Prostaglandins dilate renal blood vessels; Results in increased water and electrolyte
excretion
6. Respiratory tract - Leukotrienes promote the constriction of bronchi; Prostaglandins promote
bronchodilation
3.2 GLYCERIDES - these are glycerol-containing lipids
3.2.1. Neutral glycerides

- so named because they are nonionic and nonpolar; produced from the esterification of glycerol with one or
more fatty acids: monoglycerides; diglycerides ; triglycerides
Triglycerides (or triacylglycerol, TAG)

- serve as energy storage in adipose cells; esters of glycerol and fatty acids
a) simple triglycerides
- if all three –OH groups of glycerol molecule are esterified with the same fatty acid; have been
synthesized in the laboratory but rarely occur in nature
e.g., Glyceryl tripalmitate (Tripalmitin)
b) mixed triglyceride
- contain 2 or 3 different fatty acid components; most fats and oils are mixed TAG
e.g., CH2-O-COC17H33
CH–O-COC11H23
CH2-O-COC15H31
Glyceryloleolauropalmitate
Fats vs. Oils
- fats contain a greater proportion of saturated fatty acids than unsaturated fatty acids; so solid or semi-
solid at room temperature; beef tallow and pork lard are fats
- oils contain a greater proportion of unsaturated fatty acids than saturated fatty acids; so liquid at same
temperature; soybean oil, canola oil, peanut oil
4
- coconut oil, which is highly saturated, is an exception: this oil is a liquid not because it contains more
double bonds within the fatty acids but because it is rich in shorter-chain fatty acids, particularly lauric
acid (12:0)
- lipids obtained from animal sources are usually solids whereas oils are generally of plant origin. Hence,
we commonly speak of animal fats and vegetable oils .
A comparison of saturated and unsaturated fatty acids in some foods
Physical Properties of Lipids

- either liquid or noncrystalline solids at room temperature
- pure fats and oils are colorless, tasteless, odorless, lighter than water, poor conductors of heat and
electricity (therefore, serves as excellent insulators for the body)
- the characteristic color, odor, flavor associated with lipids are imparted to them by foreign substances
that have been absorbed by the lipid and are soluble in them. For example, the yellow color of butter is
due to the presence of carotene, taste is due to 2 compounds: diacetyl, CH3CO-COCH3, and 3-hydroxy-2-
butanone, that are produced by bacteria in the ripening of the cream.
- the melting points of fatty acids depend on both the length of their hydrocarbon chains and the degree
of unsaturation; typical saturated fatty acids are tightly packed together so they have higher melting
points than unsaturated acids with the same number of carbon atoms; cis double bonds prevent good
alignment of molecules in unsaturated fatty acids leading to poor packing and lower mp relative to
saturated or trans acid.
- the greater the degree of unsaturation the greater the reduction in melting point; this is explained by
decreased molecular attractions between carbon chains with increasing degree of unsaturation.
Chemical Properties of Lipids

1) Alkaline hydrolysis
- lipids may be hydrolyzed by alkali or by enzymes called lipases; reaction is termed saponification
because one of the products of hydrolysis is a soap, generally Na- or K- salts of fatty acids
- provides a useful analytical method for the determination of a constant, saponification number, which
is characteristic of the simple lipids
- saponification number is the number of mg of KOH required to saponify 1 g of a fat or oil; high for lipids
containing short-chain fatty acids (contains more acid molecules); low for lipids containing long-chain
fatty acids (contains fewer acid molecules) and indicates high molar mass
- experimentally,a weighed sample of fat is saponified with a standard solution of alc. KOH. Following
saponification, the excess alkali is determined by titration with standard acid
2) Halogenation
- a test for unsaturation; the amount of halogen absorbed by a lipid can be used as an index of the
degree of unsaturation; the index value is called iodine number , the number of grams of iodine that
will add to 100 g of fat or oil; the rule is: high I2 number indicates a high degree of unsaturation
- experimentally, a weighed sample of lipid is treated with an excess of the iodine reagent. After reaction
is complete, the unused iodine is determined by titration with a standard solution of Na2S2O3
3) Hydrogenation
- converts oils to fats (hardening); hydrogen is bubbled through hot oil in the presence of a nickel
catalyst; control of the degree of hydrogenation gives the various types of partially hydrogenated
vegetable products on the market today – soft margarine, solid stick margarine, and shortenings
- partial hydrogenation of unsaturated fats generates trans fats; if hydrogenation is allowed to continue
for a long period of time, glycerol and long-chain alcohols are formed (reduction of esters)
5
4) Rancidity
- the development of disagreeable odor
- a fat or oil becomes rancid when its double bonds are oxidized by oxygen and lipases furnished by
microorganisms in the air forming short-chain fatty acids and aldehydes as products which have
disagreeable odor; also responsible for the odors associated with workouts and heavy perspiration
- oxidation also occurs in the oils that accumulate on the surface of the skin during heavy exercise. The
relatively high body temperature and the presence of microorganisms on the skin promote rapid
oxidation of these oils as they are exposed to oxygen and water
a) hydrolytic rancidity
* under moist and warm conditions, microorganisms in the air furnish the lipases that catalyze the
process; hydrolysis of ester linkages occurs, liberating the volatile, low mol. wt. acids (e.g., butyricacid
from rancidity of butter)
* prevented by storing butter covered in a refrigerator
b) oxidative rancidity
* occurs in triglycerides containing unsaturated fatty acids
* highly unsaturated oils react with oxygen forming aldehydes and acids
* antioxidants may be used like Vit. E, ascorbic acid, BHA, BHT
[O] O | [O] | |
-CH=CH-  -C-H + H-C=O  HO-C=O + HO-C=O
Fat Substitute
Olestra (also known by its brand name Olean) is a fat substitute that adds no fat, calories, or
cholesterol to products. It has a sucrose base instead of the alcohol base of fat. Compared with conventional
fats, which have up to three fatty acids attached to the base, olestra has between six and eight fatty acids
attached to alcohol groups. These groups hang from a ring of sucrose molecules. The ring is completely
impenetrable to fat-removing enzymes and therefore remains indigestible, contributing zero calories. It has
been used in the preparation of traditionally high-fat foods such as potato chips, thereby lowering or
eliminating their fat content. In the late 1990s, Olestra lost its popularity due to side effects (cramping,
flatulence, loose bowels, diarrhea), but products containing the ingredient can still be purchased at grocery
stores.
6
Soaps and Detergents
Soaps are sodium or potassium salt of long-chain fatty acids; potassium soaps are more expensive but
produce a softer lather and are more soluble, used in liquid soaps and shaving creams.
- +
Soap molecule structure, CH3(CH2)16COO Na , is composed of a large nonpolar hydrocarbon portion
(hydrophobic) and a carboxylate salt end (hydrophilic)
The cleansing action of soap: (emulsification and lowering of the surface tension of water)
When soap is added to water, the hydrophilic ends of the molecules are dissolved, but the
hydrophobic ends are not and consequently form a thin film (suds) on the surface of water. When this soap
solution is brought into contact with grease or oil (most of the dirt is held to clothes by a thin film of grease or
oil), soap molecules become reoriented. The hydrophobic portions dissolve in the grease or oil and the
hydrophilic ends remain dissolved in water. Mechanical action, such as scrubbing, causes the oil or grease to
disperse into tiny droplets, and soap molecules arrange themselves around the surface of the globules forming
micelles which don’t coalesce because of repulsions between their surrounding carboxylate groups. The entire
micelle becomes water-soluble which may be washed away by a stream of water.
Detergents don’t form precipitates with ions of hard water

1. Anionic detergents – sulfates of fatty acids or sulfonate salts of hydrocarbons
2. Cationic detergents – referred to as invert soap because their water-soluble end carries a positive,
rather than negative charge; widely used in hospitals, good cleansing agents, have germicidal
properties
3. Nonionic detergents – contain polar covalent structures that provide the required water solubility;
used extensively in dishwashing liquid and on all occasions that call for absence of inorganic ions.
7
3.2 2 Phosphoglycerides (glycerophospholipids, or phosphatides)
phospholipid is a more general term
- a group of lipids containing a phosphate group; found in all living organisms; abundant in the liver,
brain, & spinal tissue and are found in the outer membranes of most cells
- contain acyl groups derived from long-chain fatty acids esterified at C1 and C2 of glycerol-3-P
- the simplest phosphoglyceride contains a free phosphoryl group and is known as phosphatidate
- when the phosphoryl group is attached to another hydrophilic group, a more complex phospho-
glyceride is formed.
e.g. phosphatidylcholine (lecithin) & phosphatidylethanolamine (cephalin)
- two of the common PL found in membranes; primary function is to act as emulsifying agent at cell
membrane surfaces since it contain both a polar and nonpolar component
- their bipolar nature is central to the structure and function of cell membranes
a) lecithin (phosphatidylcholine)
o +
- contains choline, a 4 ammonium salt, HOCH2CH2 N(CH3)3, joined to a H3PO4 residue by means of an
ester linkage
- the N in choline carries a formal positive charge and the phosphate a negative charge so that in
solution, at most pH values, lecithin exists as an internal salt or ZWITTERION
- pure lecithin is especially abundant in eggyolk and soybeans, wheat germ and yeast; also found in
brain and nervous tissue
- excellent emulsifiers and for this reason eggyolk is an excellent emulsifier to hold olive oil and water
together as mayonnaise; emulsifying agent (aids in the suspension of fats in water) in ice cream
- claims arise that lecithins should be taken as a nutritive supplement; some claims indicate it will
improve memory. There is no evidence that these supplement s are useful. The enzyme lecithinase in
the intestine hydrolyzes most of the phosphatidylcholine taken orally before it passes into body fluids,
so it does not reach body tissues. The phosphatidylcholine present in membranes is made by the liver;
thus phophatidylcholines are not essential nutrients.
8
b) cephalin (phosphatidylethanolamine or phosphatidylserine)
- the term is derived from its chief occurrence in the body, namely the head, & spinal tissue (Greek,
Kephalikos, head); found in heart and liver tissue and in high concentrations in the brain.
- in cephalins, the choline is replaced by ethanolamine, H2N-CH2CH2OH, (phophatidyl ethanolamine) or
by the amino acid serine, H2N-CH(CH2OH)-COOH, (phosphatidyl serine)
- play an important role in the process of blood clotting
3.3 NONGLYCERIDES (these are lipids not derived from glycerol)

3.3.1 Waxes
- easily melted solids, widely distributed in nature and are found in both plants and animals
- not as easily hydrolyzed as the triglyerides and therefore are useful as protective coatings
- plant waxes are found on surface of leaves and stems and protect the plant from dehydration and
invasion by harmful organisms; animal waxes are found on surface of feathers, skin, and hair.
Some common waxes Source Application
a) Beeswax honeycomb shoe polishes, candles, lipstick,
(myricyl palmitate) wax paper
C15H31COOC30H61
b) Carnauba wax Carnauba palm polishes, floor wax, automobile wax
(myricyl cerotate) (in Brazil) wax
C25H51COOC30H61
c) Spermaceti sperm whale ointments, soaps, cosmetics
(cetyl palmitate) manufacture of candles
C15H31COOC16H33
d) Lanolin wool skin ointments & lotions to aid
mixture of cholesterol retention of water which softens
& esters of several fatty acids the skin
- paraffin wax is different because it is merely a mixture of hydrocarbons and is not an ester.
3.3.2 sphingolipids
- derived from sphingosine, an 18-carbon unsaturated amino dialcohol
- can be regarded as derivatives of ceramide (core of each type of sphingolipid), a compound consisting
of sphingosine and a fatty acid
CH3(CH2)12CH = CH – CH – OH
|
H2N – CH
|
Sphingosine CH2OH
a) sphingomyelin
- the white matter of the myelin sheath, a coating surrounding the nerve cells that increases the speed
of nerve impulses and insulates & protects the nerve cells
- located throughout the body but function principally in brain and nerve tissue; found in all cell
membranes and are important structural components of the myelin sheath that surrounds and
insulates cells of the central nervous system. Their role is essential to proper cerebral function and
nerve transmission.
- may also be classified as phospholipids since they contain phosphate group
9
b) glycolipids (cerebrosides)
- occur primarily in the brain (7% of the solid matter) and in the myelin sheath of nerves
- composed of sphingosine, a fatty acid, and a sugar moiety; galactocerebrosides are almost entirely
found in the cell membranes of brain; various members of the class differ only with respect to their
constituent fatty acid
c) gangliosides
- similar to cerebrosides but contain oligosaccharide groups with one or more sialic acid residues.
- important in cell membranes as receptors for hormones, viruses, and several drugs
Diseases originating from abnormal metabolism

and accumulation of sphingoilipids
Disease Symptom Sphingolipid Enzyme
Tay-Sachs Blindness, muscles weak Ganglioside β-hexose-aminidase A
Gaucher’s Liver & spleen enlarge, Glucocerebroside β-glucosidase

MR
Krabbe’s demyelation, MR Galactocerebroside β-galactosidase
Nieman-Pick MR Sphingomyelin Sphingomyelinase

10
3.3.3 steroids
- complex derivatives of triterpenes; occur in plant and animal tissues, yeasts, and molds, but not in
bacteria, and may exist free or combined with fatty acids or carbohydrates
- for many years a great deal of controversy has surrounded various steroids. We worry about the
amount of cholesterol in the diet and the possible health effects. We are concerned about the anabolic
steroids by athletes who wish to build muscle mass and improve their performance. However,
members of this family of molecules derived from cholesterol have many important functions in the
body. The bile salts that aid in the emulsification and thus digestion of lipids are steroid molecules, as
are the sex hormones testosterone and estrone.
- all steroids have cyclopentanoperhydrophenanthrene nucleus which consists of a completely
saturated phenanthrene moiety fused to a cyclopentane ring
a) sterols
- steroids containing one, two, or three double bonds and one or more hydroxyl groups
- differ from other lipids in that they do not undergo saponification
e.g., cholesterol
- best known and most abundant (about 240 kg) steroid in the body; high occurrence in the brain and
nervous tissue; the principal constituent of gallstones from which it can be isolated as a white
crystalline solid. Its name is derived from this source (Greek, chole – bile; steros – solid)
- found in the membrane of most animal cells; readily soluble in the hydrophobic region of membranes
and is the principal membrane lipid involved in regulation of the fluidity of the membrane.
- Cholesterol plays a vital biochemical role in chemical synthesis within the human body; it is the
starting material for the synthesis of numerous steroid hormones, vit. D, and bile salts; its presence in
the body is essential to life
- Cholesterol is not necessary in the diet. The human body, mainly within the liver, synthesizes about 1
gram of cholesterol each day, an amount sufficient to meet the body’s biosynthetic needs.; when it is
ingested, the amount synthesized by the body is reduced; however, the reduction is less than the
amount ingested so that the body cholesterol level increases with dietary cholesterol level.
- Medical science now considers high blood cholesterol, along with high blood pressure and smoking, as
the major risk factors for cardiovascular disease (CVD). High blood cholesterol contributes to
atherosclerosis, which is characterized by the buildup of plaque along the inner walls of the arteries.
Plaque is a mound of lipid material mixed with smooth muscle cells and calcium; much of the lipid
material in plaque is cholesterol. Cholesterol, in combination with other substances, appears to coat
the arteries, resulting in a narrowing. As this narrowing increases, more and more pressure is
necessary to ensure adequate blood flow. The pressure in the blood vessels increases, and high blood
pressure (hypertension) develops. Hypertension is also linked to heart disease.
11
b) bile acids/ bile salts
- salts of bile acids are the most important constituents of human bile; bile is produced by the liver,
stored in the gall bladder, and secreted into the intestine
- a bile salt is an emulsifying agent that makes dietary lipids soluble in the aqueous environment of the
digestive tract; main function is to facilitate the absorption of fats through the wall of the intestine
- cholic acid is the most abundant bile acid
- bile salts are cholesterol oxidation products where cholesterol is oxidized to carboxylic acid which is
then bonded to an amino acid by amide linkage; the two principal bile salts are sodium glyocholate
(glycine is the amino acid) and sodium taurocholate (taurine is the amino acid).
c) steroid hormones
- a hormone is a chemical messenger secreted by specific glands and carried by the blood to a target
tissue, where it triggers a particular response. Hormones serve as a means of communication between
various tissues; hormones, together with the central nervous system(CNS), are the regulators of body
reactions like metabolism, growth and development, etc.
adrenocortical hormones
- produced by the outer part, or cortex, of the adrenal glands, small organs on top of each kidney
- regulate numerous biochemical processes in the body; effect the metabolism of foodstuffs and control
+ +
inflammation and allergies (glucocorticoids); maintain the proper balance of electrolytes Na and K
ions in cells (mineralocorticoids)
- adrenal hormones are widely used in the treatment of rheumatic fever and rheumatoid arthritis.
` Aldosterone Cortisol Cortisone Prednisolone

(a mineralocorticoid) (a glucocorticoid) (an anti-inflammatory drug) (an anti-inflammmatory drug)
sex hormones
a. androgens - the male sex hormones, the most important is testosterone; synthesized in the testes and
o o
adrenal cortex; regulate the development of 1 and 2 male sex characteristics
b. estrogens - the female sex hormones; synthesized in the ovaries and adrenal cortex; regulate the
o o
development of 1 and 2 female sex characteristics and for regulation of the menstrual cycle; also
stimulate the development of the mammary glands during pregnancy and induce estrus (heat) in animals.
c. progestins - the pregnancy hormones; for normal pregnancy; produced in the ovaries and in the placenta,
it is responsible for both the successful initiation and completion of pregnancy;
it prepares the lining of the uterus (endometrium) for implantation of the ovum. Once the egg is attached,
progesterone is involved in the development of the fetus and also plays a role in the suppression of further
ovulation during pregnancy
Estradiol Testosterone
(the principal estrogen; (the principal androgen; (the principal progestin;
for female sex characteristics) for male sex characteristics) for normal pregnancy)
12
- increased knowledge of the structures and functions of sex hormones has led to the development of a
number of synthetic steroids; among the best known are oral contraceptives and anabolic agents.
- anabolic steroid abuse can result in a wide range of harmful side effects including some that are
physically unattractive such as acne and breast development in men; the side effects can also be life-
threatening, such as liver cancer and heart attacks.
Norethynodrel RU-486 Methandrostenolone

(a synthetic progestin) (mifepristone; a synthetic abortion drug) (a synthetic tissue-building steroid)
3.4 COMPLEX LIPIDS (lipids that are bonded to other types of molecules)
3.4.1 phospholipids
- see phosphoglycerides, & sphingomyelin;
- fatty acids, glycerol, H3PO4 and a nitrogenous base on hydrolysis
3.4.2 glycolipids
- see cerebrosides, & gangliosides; fatty acids, sphingosine, and a carbohydrate on hydrolysis
3.4.3 lipoproteins
- responsible for the transport of other lipids in the body; lipids are only sparingly soluble in water, and
the movement of lipids from one organ to another through the blood stream requires a transport
system that operates via plasma lipoproteins
- lipoprotein particles consist of a core of hydrophobic molecules such as triglycerides or cholesterol
esters (cholesterol esterified to fa’s). The shell around the core consists of polar lipids and proteins
Four major classes:

a) chylomicron
- transports dietary TAG, cholesterol, etc. from the intestines to other tissues (adipose tissue and liver),
except kidney; 90% triglyceride + 1% protein
b) very low density lipoprotein (VLDL)
- bind triglycerides synthesized in the liver and carry them to adipose tissues and other tissues for
storage; 50% triglyceride + 10% protein
c) low density lipoprotein (LDL)
- carry cholesterol to peripheral (adipose) tissues and help regulate cholesterol levels in those tissues;
regulates de novo synthesis of cholesterol; 10% triglyceride + 20% proteins
- liver LDL receptors enable large amounts of cholesterol to be removed from the blood, thus ensuring
low concentrations of cholesterol in plasma. Other factors being equal, the person with the most
lipoprotein receptors will be the least vulnerable to a high-cholesterol diet and will have the least
likelihood of developing atherosclerosis.
d) high density lipoprotein (HDL)
- transports cholesterol from peripheral tissues to the liver; 5% triglyceride + 50% protein
13
- there is evidence that high levels of HDL in the blood help to reduce the incidence of atherosclerosis.
This may be due to the fact that HDL carries cholesterol from the peripheral tissues back to the liver. In
the liver, some of the cholesterol is used for bile synthesis and secreted into the intestine, from which
it is secreted.
* High VLDL and low HDL are risk factors in atherosclerosis and predisposes toward strokes
and coronary infarction
* When the level of LDL is high in relation to the HDL there is a high risk of coronary disease
(LDL/HDL above 4.0)
Structure of Cell Membranes

Living cells contain ~10,000 kinds of molecules in an aqueous environment confined by a cell
membrane A cell membrane is a structure that separates a cell’s aqueous-based contents from the aqueous
environment surrounding the cell. Besides its “separation” function, a cell membrane also controls the
movement of substances into and out of the cell. Up to 80% of the mass of a cell membrane is lipid material;
hence the consideration of cell membranes in the chapter on lipids. Cell membranes contain various
phosphoacylglycerols (phospholipids) and sphingolipids. The “head and two tail” structure of these lipids is of
key importance to an understanding of the lipid bilayer structural feature of the cell membranes. A lipid
bilayer is ~6-9 nanometers, two-layer thick structure of lipid molecules aligned so that the nonpolar tails of the
lipids form the interior of the structure and the polar heads form the outside surfaces.
Cholesterol molecules are also components of cell membranes. They regulate membrane fluidity.
Because of their compact shape cholesterol molecules fit between the fatty acid side chains of the lipid bilayer,
restricting movement of the fatty acid side chains and making the bilayer more rigid.
Proteins are also components of the lipid bilayers. They are responsible for moving substances such as
nutrients and electrolytes across the membrane, and they also act as receptors that bind enzymes, hormones,
and neurotransmitters.
14
Small carbohydrate molecules are also components of cell membranes. They are found on the outer
membrane surface covalently bonded to protein molecules (a glycoprotein) or lipid molecules (a glycolipid).
They function as markers, substances that play key roles in the process by which different cells recognize each
other.
Characteristics of cell membrane

1. Fluidity - increasing percentage of unsaturated fats leads to more fluidity of the membrane. Lateral
movement of phospholipids is rapid. Flip-flop, from one side to the other is rare.
2. Selective permeability - the hydrophobic nature of the membrane makes it impenetrable to the transport of
ionic and polar substances. Membrane proteins regulate passage of ionic and polar substances by
binding to the polar compound or by providing a channel.
3. Self-sealing capacity - a break in the membrane immediately and spontaneously seals.
4. Asymmetry - bulkier molecules occur more often in the inner side of the membrane.
5. Strong and rigid
Membrane Transport Mechanisms

1. Passive transport – there is no direct energy input
a) simple diffusion – molecules move through a membrane down a concentration gradient (toward
lower concentration)
b) facilitated diffusion – molecules move through protein channels in membrane; permease, a
membrane protein assists in diffusion
2. Active transport – require energy
+ +
a) primary – energy is provided by ATP (e.g., Na - K pump system)
b) secondary – concentration gradients generated by the primary active transport are used to move
+ + +
substances across membranes (e.g., Na gradient from Na - K pump system is used to transport
glucose in kidney tubules.
15
Saponifiable and Nonsaponifiable Lipids
- saponifiable lipids produce fatty acids upon treatment with NaOH
- include fats/oils, waxes, phospholipids (glycerophospholipid, sphingolipid), and glycolipids
- nonsaponifiable lipids include steroids and terpenes, can’t be hydrolyzed by NaOH
3.5 MISCELLANEOUS LIPIDS

- Vitamin = “vital amine,” from an early belief that vitamins might all be amines
- the body cannot make vitamins; they must be in the diet
- the term vitamin applies to any compound or a closely related group of compounds satisfying the
following criteria:
• it is organic rather than inorganic or an element
• it cannot be synthesized at all (or at least in sufficient amounts) by the body
• its absence causes a specific vitamin deficiency disease
• its presence is essential to normal growth and health
• it is present in foods in small concentrations, and it is not a carbohydrate, a saponifiable lipid, an
amino acid, or a protein
- function in the body either as precursors for coenzymes or as coenzymes themselves. Most of the
nutritionally required minerals function as cofactors to enzymes
3.5.1 Terpenes or isoprenoids

- are polyenes, alkenes with several double bonds, are found in nature; built from one or
more five-carbon units called isoprene, CH2=CCH3CH=CH3
- steroids, chlorophyll & carotenoid pigments, fat-soluble vitamins.
3.5.2 Fat-soluble vitamins
- fat-soluble vitamins are largely hydrocarbon-like, and water-soluble vitamins are polar or ionic
- fat-soluble vitamins occur in the lipid fractions of their sources
- their molecules have double bonds or phenol rings, so oxidizing agents readily attack them; hence,
these vitamins are destroyed by prolonged exposures to air or to the organic peroxides that develop in
fats and oils turning rancid. These are actually good properties; because the fat-soluble vitamins are
easily oxidized, they destroy oxidizing agents (which are involved in the development of coronary
heart disease, genetic mutations, and cancer)
a) Vitamin A (retinol)
- a primary alcohol of molecular formula C20H30O; occur only in the animal world, where the best
sources are cod-liver oil and other fish-liver oils, animal liver and dairy products
- provitamin A is found in the plant world in the form of carotenes. Provitamins have no vitamin
activity; however, after ingestion in the diet, β-carotene is cleaved at the central carbon-carbon double
bond to give 2 molecules of Vit. A.
- the major action of Vit. A is probably on epithelial cells, particularly those of the mucous membranes
of the eye, oral cavity, digestive, respiratory, reproductive and genitourinary tracts. Without adequate
supplies of vitamin A these membranes become hard and dry (keratinized)
16
- though harmless, excessive β-carotene ingestion makes the skin yellow or orange. In distinction to
observation in cases of jaundice, the sclera remains white
- Vit. A (retinol) is oxidized to retinal, or vitamin A-aldehyde, which combines with opsin, a protein, to
form rhodopsin, the light-seeing pigment in the retina.
- most obvious effects of vit. A deficiency is on the eye. The cells of the tear glands become keratinized
and stop secreting tears, & the external surface of the eye becomes dry, dull, and often scaly. Without
tears to remove bacteria, the eye is susceptible to serious infection, which if not treated on time,
blindness results  xerophthalmia
- a less serious condition is night blindness, the inability to see dim light or to adapt to subdued light
b) Vitamin D (“solar vitamin”)

0 2+
- a 2 alcohol; C28H44O; the antirachitic vitamin; primary effect is on Ca metabolism, it increases the
2+
absorption of Ca from the intestinal tract; necessary for the normal calcification of bone tissue
- compounds with antirachitic activity:
* Vitamin D2 or ergocalciferol (vegetable origin)
* Vitamin D3 or cholecalciferol (animal origin); fish-liver oils – richest source
Ergocalciferol (D2) Cholecalciferol (D3)
- pigment in the skin, 7-dehydrocholesterol, is a provitamin D; when irradiated by the sunlight becomes
converted to Vit. D3
- humans exposed to sunlight year-round do not require dietary Vit. D
c) Vitamin E
- a group of about seven compounds of similar structure; of these, α-tocopherol has the greatest
potency; tocopherol  Greek, promoter of childbirth; the antisterility vitamin
- functions in the body as an antioxidant in that it inhibits the oxidation of unsat’d fatty acids by O2
17
- occurs in fish oil, cottonseed and peanut oil, green leafy vegetables; the richest source is wheat germ
oil
α-tocopherol
d) Vitamin K
- essential for the synthesis of prothrombin in the liver; the antihemorrhagic vitamin
Vitamin K2
(n may be 5, 6, or 8)
- synthesized by intestinal bacteria

- deficiency may occur during the first few days after birth, because newborns lack the intestinal
bacteria that produce Vit. K and because they have no store of Vit. K (it does not cross the placenta)
- hence, all newborns are given vitamin K injection to prevent hemorrhagic disease
- deficiency may also occur following antibiotic therapy that sterilizes the gut
18
19
20
Lipids
CHEM2N LAB CLASS BSN1
Presented by
JHON ABRIEN S. SOLIZA, RCh

Lipids
• Lipid comes from the Greek word “lipos” meaning fat.
• Consist of fatty acids
• insoluble in water
• serve as energy storage
• membranes components
• aid absorption of fat-soluble vitamins (A, D, E, K)
• aid enzyme activities
• Messengers
-Primary: Hormones
-Secondary: mediate hormonal response
• forms layers of fats to insulate the body
Fig 20.1, p.501
Fatty Acids
• Most abundant are

palmitic acid
(16:0), stearic acid
(18:0), and oleic
acid (18:1)
• Are amphipathic
Fatty Acid Notation
• Delta Nomenclature
/ C – SYSTEM
Fatty Acid Notation
• Omega
Nomenclature/ n-
system
Table 20.1, p.496
Fatty Acids
Melting COOH
Carbon Atoms/ Common Point COOH
Double Bonds* Name (°C)
Saturated Fatty Acids
COOH
12:0 Lauric acid 44
14:0 Myristic acid 58
16:0 Palmitic acid 63
18:0 Stearic acid 70
20:0 Arachidic acid 77
Unsaturated Fatty Acids
16:1 Palmitoleic acid 1
18:1 Oleic acid 16
18:2 Linoleic acid -5
18:3 Linolenic acid -11
20:4 Arachidonic acid -49
Packing of Saturated vs Unsaturated Fatty Acids
• Larger surface area

• more interaction with each other • Presence of double bond in kink structure give a
• higher IMF smaller surface area
• solid or semi solid at room temp • Less interaction with each other
• higher melting point • Lower IMF
• Liquid at room temp
• Lower melting point
Lodon dispersion forces is the dominant IMF in fatty acid since it contains long chain of nonpolar molecule
Classification of Lipids
• Simple Lipids – Fatty Acids +
Alcohol
– TAG (Triacylglycerol)
Triglyceride (triacylglyceride): an ester
of glycerol with three fatty acids
Triglycerides
• Physical properties depend on the fatty acid
components
– More carbons: higher melting point
– More saturated (fewer C=C): higher melting point
– Oils:
• More unsaturated fatty acids
• Liquid at room temperature
– Fats:
• Primarily saturated fatty acids
• Semisolids or solids at room temperature
Triglycerides
• Melting points related to 3-D shape of
triglyceride
– Saturated fatty acids can pack closely together
• More London dispersion forces between chains
• Higher melting points (above room temperature)
– Unsaturated fatty acids have cis double bonds
• Bend in chain prevents close packing
• Fewer London dispersion forces between them
• Lower melting points (below room temperature)
Hydrogenation
• Can convert liquid oil to solid fat by adding H2

to double bonds by using H2/catalyst
– Can control hardening to produce fats of a desired
consistency
– Examples: Crisco, Spry, Dexo, etc.
– Margarine produced by partial hydrogenation of
polyunsaturated oils derived from corn, cottonseed,
peanut, and soybean oils
Iodine or Bromine Test for
Unsaturation
• Add Br2 (or I2) to C=C.
• The more Br2 or I2 you add, the greater the

number of double bonds in the fat or oil
• Iodine number is a measure of unsaturation.

Soaps
• Natural soaps are prepared by boiling lard or other animal
fat with NaOH, in a reaction called saponification (Latin,
sapo, soap)
O
O CH 2 OCR
saponification
RCOCH + 3N aOH
O
CH 2 OCR CH 2 OH O
- +
A triglyceride CHOH + 3RCO N a
(a triester of glycerol) Sodium soaps
CH 2 OH
1,2,3-Propanetriol
(Glycerol; Glycerin)
Soaps
• Soaps clean by acting as emulsifying agents
– their long hydrophobic hydrocarbon chains cluster
so as to minimize their contact with water
– their polar hydrophilic carboxylate groups remain in
contact with the surrounding water molecules
– driven by these two forces, soap molecules
spontaneously cluster into micelles
Waxes
• High molecular-weight esters
• Paraffin wax are special types of waxes which aren’t
esters. They are high molecular weight alkanes mainly
used for candles.
46 C total for triacontyl palmitate

Complex Lipids
Fatty Acids + Alcohol + additional Group. One of the hydroxides

reacts with a different group.
• Phospholipids
• Glycolipids
• Lipoproteins
• Phospholipids
– contain an alcohol, two fatty acids, and a phosphate
Complex Lipids ester
– in glycerophospholipids, the alcohol is glycerol
– in sphingolipids, the alcohol is sphingosine
Membrane bilayer
• Hydrophilic head outside
• Hydrophobic tails inside
Simple lipids Complex lipids found in membranes
Fig 20.1, p.501

Glycerophospholipids
• A phosphatidic acid
palmitic acid
O
glycerol
O CH2
O CH -
oleic acid O
-
O CH2 -O-P-O
O
– Fatty acid attached to C-2 is always unsaturated
– Can also add small alcohol to the phosphate to
make a glycerophospholipid
Glycerophospholipids
Name of
Name and Formula Glycerophospholipid
ethanolamine cephalin
HOCH2CH2 NH2
choline lecithin
+
HOCH2CH2 N(CH 3)3
serine cephalin
-
HOCH2CHCOO
+
NH3
inositol OH phosphatidylinositol
OH
HO OH
HO OH
Sphingolipids
• Found in the myelin sheath of
nerve axons
– Sphingomyelin deterioration found in
MS
• Contain sphingosine, a long-chain
aminoalcohol
(CH 2 ) 12 CH 3 (CH 2 ) 12 CH 3 (CH 2 ) 12 CH 3
HO HO O HO O
N H2 N HCR N HCR
O- +
OH OH OPOCH 2 CH 2 N(CH 3 ) 3
Sphingosine A ceramide
O
(an N-acylsphingosine)
A sphingomyelin
Glycolipids
• Glycolipid: complex lipid that contains a sugar
– Sugar is glucose or galactose
– Cerebrosides found in brain and nerve synapses
(CH2 ) 12CH 3
a ceramide
a unit of
b-D-glucopyranose HO O
H OH NHCR
HO
HO O
HO a b-glycosidic bond
H
OH
H H
Transport of Lipids
• Lipoproteins
– Classified by their density and function
Lipoproteins
• Cholesterol, along with fats, are transported
by lipoproteins
Composition (% dry weight)
Cholesterol Phospho- Tri-
Lipoprotein Proteins and esters lipids glycerides
High-density 33 30 29 8
lipoprotein (HDL)
Low-density 25 50 21 4
lipoprotein (LDL)
Very-low density 10 22 18 50
lipoprotein (VLDL)
Chylomicrons 1-2 8 7 84
• Cholesterol forms plaque
deposits on inside of blood
vessels (atherosclerosis)
• Narrows blood vessel
diameter
• Lowers blood flow
• Can lead to heart attack,
stroke, kidney disfunction or
other problems
Derived Lipids
• Steroids
• Terpenes
• Eicosanoids
• fat soluble vitamins
Steroids
• Steroids: a group of plant and animal lipids that have a
steroid ring structure
C D
A B
Cholesterol
• Cholesterol is the most abundant steroid in
the human body, and also the most
important
– Component in animal plasma membranes
– Precursor of all steroid hormones and bile acids
HO
Steroid Hormones
• Androgens: male sex hormones
– synthesized in the testes
– responsible for the development of male secondary sex
characteristics
H3 C OH H3 C O
H3 C H3 C
O HO
Testosterone Androsterone
Steroid Hormones
• Among the synthetic anabolic steroids are
H 3C CH3 H3 C OH H3C O
OH
H3 C
H3 C CH 3 H3 C
O O O
Methandienone Methenolone 4-Androstene-3,17-dione
Steroid Hormones
• Estrogens: female sex hormones
– synthesized in the ovaries
– responsible for the development of female
secondary sex characteristics and control of
the menstrual cycle
CH 3
H3C C=O H3C OH
H 3C
O HO
Progesterone Estradiol
Steroid Hormones
• Progesterone-like analogs are used in oral contraceptives
CH3
N
H3 C OH
H3C C CCH3
"Nor" refers to
the absence of a
methyl group here H C OH
3 C CH
O
Mifepristone
(RU486)
O
Norethindrone
Steroid Hormones
• Glucorticoid hormones
– synthesized in the adrenal cortex
– regulate metabolism of carbohydrates
– involved in the reaction to stress
CH 2 OH
– decrease inflammation OH
O C=O
CH
H3 C H
H H
O
Aldosterone
Bile Salts
• Bile salts, the oxidation products of cholesterol
– synthesized in the liver, stored in the gallbladder,
and secreted into the intestine where they emulsify
dietary fats and aid in their absorption and digestion
O O
HO NH HO NH
COO-
2-
SO3
HO OH HO OH
Glycocholate Taurocholate
(from glycine) (from taurine)
Prostaglandins
• Prostaglandins are synthesized in response to
specific physiological triggers
• Made from membrane-bound 20-carbon
polyunsaturated fatty acids such as arachidonic
acid
9 8 6 5
COOH
11 12 14 15
Arachidonic acid
Eicosanoids 9
COOH
• are signaling 11 15
Aspirin and other
NSAIDs inhibit
Arachidonic acid
molecules which this enzyme
are derivatives of 2O2 cyclooxygenase (COX)

O
arachidonic acid 9
COOH
PGG2
(carboxylic acids O 11
15
with 20 carbon OOH
atoms). O
9
HO
9
COOH COOH
15 15
11 11
HO HO
OH OH
PGE2 PGF2 a
Prostaglandins
• Prostaglandins:
• play a key role in the generation of the inflammatory
response. Their biosynthesis is significantly increased in
inflamed tissue and they contribute to the development of
the cardinal signs of acute inflammation.
• acts as vasodilators - they widen blood vessels. They also
inhibit platelet aggregation. 7 5 3
1
9
6 2
COOH
8 4
10
12 14 16 18 20
11
13 15 17 19
Thromboxanes
• Thromboxanes are also derived from
arachidonic acid
• acts as vasoconstrictors – they can make the
blood vessels narrower.
9
8 1
10
O COOH
11 15 20
O 12
OH
Thromboxane A
TERPENES
• are aromatic lipids found in many
plants that are multiple of
isoprene units. Terpenes are non
– saponifiable meaning there are
no acid functional group in the
chain.
Fat soluble
vitamins
• Vitamins A, D, E and K
• Vitamin A is best known for its vital role in maintaining
vision. It’s also essential for body growth, immune
function, and reproductive health.
• vitamin D is the maintenance of calcium and phosphorus
levels in blood. It benefits bone health by promoting the
absorption of these minerals.
• Vitamin E’s key role is to serve as an antioxidant,
protecting cells against free radicals and oxidative
damage.
• Vitamin K is vital for blood clotting and supports bone
health.
Tay-Sachs
disease
• is an inherited metabolic
disease caused by the harmful
buildup of lipids in various cells
and tissues in the body. It is
part of a group of genetic
disorders called the
GM2 gangliosidoses.
• Tay-Sachs and its variant form
are caused by a deficiency in
the enzyme hexosaminidase A.
Affected children appear to
develop normally until about
age 6 months and then begin to
show symptoms
Fabry’s disease
• (also called alpha-galactosidase-A
deficiency) is caused by the lack of or faulty
enzyme needed to metabolize lipids, fat-like
substances that include oils, waxes, and fatty
acids.
• The mutated gene allows lipids to build up to
harmful levels in the autonomic nervous
system (which controls involuntary functions
such as breathing and digestion),
cardiovascular system, eyes, and kidneys.
Gaucher disease
• Gaucher disease is one of the inherited metabolic

disorders known as lipid storage diseases. Lipids
are fatty materials that include oils, fatty acids,
waxes, and steroids (such as cholesterol and
estrogen). People with Gaucher disease either do
not produce enough of the enzyme
glucocerebrosidase needed to break down lipids or
have enzymes that do not work properly. Fatty
materials can accumulate in the brain and other
organs.
• General symptoms may begin in early life or
adulthood and include skeletal disorders and bone
lesions that may cause pain and fractures, enlarged
spleen and liver, liver malfunction, anemia, and
yellow spots in the eyes.
• There are three common clinical subtypes of
Gaucher disease
Niemann-Pick
disease
• refers to a group of inherited metabolic
disorders known as lipid storage
diseases. Lipids (fatty materials such as
waxes, fatty acids, oils, and cholesterol) and
proteins are usually broken down into
smaller components to provide energy for
the body. In Niemann-Pick disease, harmful
quantities of lipids accumulate in the brain,
spleen, liver, lungs, and bone marrow.
• Types A and B are caused by a missing or
malfunctioning enzyme called
sphingomyelinase.
• type C is a rare inherited disease
COLEGIO SAN AGUSTIN – BACOLOD
College of Health and Allied Professions CHEM2N LABORATORY ACTIVITY
Nursing Program
Activity 4
Bicarbonate-Carbonic Buffer System
A buffer is a solution that can resist pH change upon the addition of an acidic or basic
components. It is able to neutralize small amounts of added acid or base, thus maintaining the
pH of the solution relatively stable.
Buffering in blood is crucial to our survival. The pH of blood must be kept constant for
normal body functions to work. If blood becomes too acidic, or too basic, then enzymes and
proteins are unable to function. Normal blood pH is 7.4. If it drops below 6.8, or rises above 7.8,
respiratory and cardiac function are compromised, the blood-clotting process changes, and death
may occur.
Red blood cells play an important role in the removal of excess hydrogen ions in the body.
This is achieved by a carbonic acid/Bicarbonate buffering system. This buffer system can be
represented as an equation:
This buffer works well because concentrations of the buffer components HCO3 - and CO2
(formed from H2CO3) are much greater than concentration of H+ ions. This means that changes
in the concentration of H+ ions have little effect on the pH of blood.
Other body organs play important roles in this buffer system. The lungs get rid of most of
the H+ ions produced by metabolism by removing carbon dioxide and driving the reaction
forward. The kidneys also remove H+ ions that are excreted in urine. The kidneys are also
involved in regulation of pH of body fluids through a complex interaction of H+, HCO3 - , H2O, CO2
and ions such as Na+.
OBJECTIVES
This activity should enable the students to:

1. Learn how buffer solution works
2. Importance of buffer systems in our body
3. Learn how to create a buffer solution
Materials :
• purple camote leaves juice • 2 plastic cup or clear glass (garapon or

• teaspoon baso) approximately 250-500mL
capacity (clear not colored)
• 1 Sodium bicarbonate tablet 650mg
(crushed into powder form)
• Medicine Dropper
• 5mL syringe
• Clear soda (Sprite or 7Up, for example)
(approximately 0.035M as carbonic acid)
JASSoliza/WPalacios/GDalipe/ Page 1 of 4 2nd Sem 2021-2022

Nursing Program
Follow the procedure on the link bellow:

making camote leaves pH indicator
https://www.youtube.com/watch?v=_pKbtNQVU0s
What you have in each cup is a solution of anthocyanin
(made from boiling purple camote leaves), which is an acid-base indicator. It turns blue in the
presence of high pH and pink in the presence of low pH. In between, it turns a variety of colors.
Right now, it should be a light purple, which indicates a pH of roughly 7.
Procedure:
1. using the 5mL syringe draw about 10 syringe full of the purple camote leaves Juice
Indicator into 2 clear glass/plastic cups to make approximately 50 mL.
2. Add crushed sodium bicarbonate tablet to one of the clear glass. You should see the color
change towards green. That is because the bicarbonate ion in the baking soda is a base.
The green color is anthocyanin’s reaction to the higher pH. Label this container “Buffer”.
3. Label the other clear glass/plastic cups “Control.”
4. Use the same syringe to add the Clear soda Sprite to the “Buffer” beaker that you just put
the baking soda in. Use that tablespoon to stir the solution. Continue to add Sprite one
syringe at a time (stirring in between) until the color of the solution roughly matches the
color of the solution the control (the one you haven’t added anything to). This sample
now has a mixture of an acid (carbonic acid from the Sprite) and base (bicarbonate from
the baking soda). This is the bicarbonate buffer.
5. You now have samples, each at roughly the same pH. One has a buffer solution, the other
does not.
6. Take the medicine dropper or syringe and add two drops of vinegar to the beaker labeled
“Control” that does not have the buffer. Swirl the glass to mix the vinegar in the solution.
a. Record: Note the color.
7. Next, repeat step 6 with the “Buffer” container. Record: Note the color change, if any.
8. Alternatively add two drops of vinegar to each solution, swirling in between. Continue
until each solution changes color.
a. Record how many drops were added to each solution.
b. Record: Compare how quickly the bicarbonate buffer solution changes colors to
how quickly the other solution changes colors.
9. Clean everything up.
10. Make a video presentation on every process and observation make sure to upload this
or comment in NEO submission.

Nursing Program
Respond to the following:
1. Explain any differences you saw between how quickly each solution changed color.
2. How does this relate to what we’ve discussed about buffers?
3. Why would buffers be helpful in the body? Your answer should refer to the term
homeostasis
4. Create a flow chart of boxes illustrating each step of this activity and the color reaction of
each beaker. Labels should help a reader understand what is happening. It should be
colored.
5. What is alkalosis?
6. What could lead to alkalosis in the body?
7. What is acidosis?
8. What could lead to acidosis?
9. What is the conjugate base and the acid in the buffer solution?
References
https://chem.libretexts.org/Bookshelves/Physical_and_Theoretical_Chemistry_Textboo
k_Maps/Supplemental_Modules_(Physical_and_Theoretical_Chemistry)/Acids_and_Bas
es/Buffers/Introduction_to_Buffers
https://www.uwa.edu.au/study/-/media/Faculties/Science/Docs/Buffering-systems-in-
the-human-body.pdf

Nursing Program
Name: ____________________________________________ Section:________

Date Performed: ________________________ Group No.: ______ Rating: ________
ACTIVITY NO. 3
Show your solution :
From the preparation above What is pH of the buffer?

assuming no volume change upon addition of sprite
Ka of carbonic acid = 4.5 × 10−7
Write your observations in steps 2-8 of the procedure attach pictures of the color change
record each color change of the solution
the number of drops to change the color of the control and the buffer
CONCLUSION:

Nursing Program
Activity 5
Protein denaturation
Proteins are essential for all living things to function. They are large molecules made up
of long chains of amino acids. Depending on the types of amino acids they have, proteins fold in
very specific ways. The way they fold controls what the proteins are able to do. Proteins help
move other molecules, respond to signals, make reactions happen more quickly, and replicate
DNA, among other things. However, if proteins lose their specific folded shape, they are not able
to work properly.
Proteins require specific conditions to keep their shape. For example, most proteins in
our bodies rely on us to keep a warm (but not hot) body temperature, stay hydrated, and take in
enough of specific nutrients like salt. If our bodies aren’t able to maintain these conditions, some
of our proteins may not function as well, or at all. Most organisms actually produce special
proteins called “molecular chaperones” that help other proteins and molecules continue to work
even if conditions are becoming difficult to tolerate.
When a protein is exposed to conditions too far outside of a range it can tolerate, that
protein’s shape will come undone. This is called “denaturing” (basically, breaking) a protein.
Source: Karla Moeller. (2018, May 29). Breaking Proteins. ASU - Ask A Biologist. Retrieved
March 11, 2022 from https://askabiologist.asu.edu/activities/breaking-proteins
OBJECTIVES
This activity should enable the students to:

1. Learn how proteins reacts to certain conditions
2. Importance of proteins in our body
3. Learn how to break proteins.
Materials :
2 Eggs 2pcs 5mL syringe

Spoon, Fork Stove
Alcohol Frying Pan
Vinegar Spatula
Water Tissue
Glass containers/ plastic Cups (5)

Nursing Program
Procedure:
Note: use 1 syringe only for egg white alone the other syringe wash it with water before drawing
alcohol and vinegar
Preparation of Egg Albumin Solution
• Add 5 mL (1 full draw of syringe) of Egg whites in container #1

• Add 45 mL (9 full draw of syringe) of water
• Mix slowly by swirling the mixture
• Set aside as and label as negative control
Effect of Mechanical Agitation
• Add 5 mL of Egg whites in container #2

• Beat the egg whites with fork until color change
• Compare with negative control
Effect of Heat
• Use hot water

• Add 5mL of egg white in the pan
• Stir slowly using fork
Effect of Alcohol
• Add 2mL of the egg albumin solution to container #4

• Add 3-5mL of alcohol
• Mix thoroughly using fork. Stand for 5 minutes.
Effect of Acid
• Add 2mL of the egg albumin solution to container #5

• Add 3-5mL of vinegar.
• Mix thoroughly. Stand for 5 minutes.
Respond to the following:
1. What other things change color when their proteins are denatured?
2. Why might a living organism want to keep their proteins from denaturing?
3. In this activity, why was it important to have egg whites that we did not cook or add
alcohol to?
4. How did the proteins change when they were denatured?
5. What is the disadvantage of protein denaturation?

Nursing Program
6. Can denatured protein still function?
7. Can water denature proteins?
8. What happens if a muscle protein is denatured?
9. Is denaturation pH reversible?
10. Why is denaturation harmful?
11. Why is denaturation important?

Nursing Program
Name: ____________________________________________ Section:________

Date Performed: ________________________ Group No.: ______ Rating: ________
ACTIVITY NO. 5
Record your observation and comparison to negative control here:

Note: paste pictures of your comparisons
CONCLUSION:

VII. METABOLISM
B. CARBOHYDRATE METABOLISM
The process in brief:

1. Starch is the principal carbohydrates ingested by humans. Digestion of starch begins in the mouth
where the enzyme ptyalin (an amylase and maltase) catalyzes the hydrolysis of starch into dextrins.
Sucrose and lactose are not digested in the mouth.
2. Ptyalin continues to function as food passes through the esophagus, but is quickly inactivated when it
comes in contact with the acidic environment of the stomach. Very little carbohydrate digestion occurs
in the stomach; acid-catalyzed hydrolysis proceeds too slowly at body temperature to be effective.
3. The primary site of carbohydrate digestion is the small intestine where another amylase, amylopsin
converts the remaining starch molecules along with the dextrins to maltose. Maltose is then cleaved
into 2 glucose units by maltase; sucrose, to glucose and fructose by sucrase; and lactose, to glucose
and galactose by lactase.
4. Ultimately, the complete hydrolysis of polysaccharides and disaccharides produce 3 monosaccharide
units: glucose, fructose, and galactose, which are then absorbed by active transport through the walls
of the small intestine into the bloodstream.
5. Following absorption the monosaccharides are carried by the portal vein to the liver where galactose
and fructose are enzymatically converted to glucose.
6. The glucose may then pass into the general circulatory system to be transported to the tissues or
converted to glycogen reserve in the liver.
7. The glucose in the tissues may be a) oxidized to CO 2 and H 2 O (ATP)
b) converted to fat
c) converted to muscle glycogen
Blood-sugar level:
- the proper functions of the body are dependent on precise control of the glucose concentration in the
blood.
- the normal fasting level of glucose in the blood is 70-90 mg/100 ml.
Abnormal conditions:
1) hypoglycemia
- condition resulting from a lower than the normal blood-sugar level (below 70 mg/100 ml)
- extreme hypoglycemia, usually due to the presence of excessive amounts of insulin, is characterized by
general weakness, trembling, drowsiness, headache, profuse perspiration, rapid heart beat, lowered
blood pressure and possible loss of consciousness. Loss of consciousness is most likely due to the lack
of glucose in the brain tissue, which is dependent upon this sugar for its energy.
2) hyperglycemia
- higher than the normal level (above 120 mg/100 mL); when the pancreas does not secrete enough
insulin
- may temporarily exist as a result of eating a meal rich in carbohydrates.
- extreme hyperglycemia, the renal threshold (160-170 mg/100 mL) is reached and excess glucose is
excreted in the urine
1
Hormone control of carbohydrate metabolism
1) Insulin – secreted by the pancreas and functions to lower blood-sugar level by enhancing the formation of
glycogen from glucose (glycogenesis)
- a deficiency of insulin (hypoinsulinism) results in a permanent hyperglycemic condition known as
diabetes mellitus. If little or no insulin is present, glucose cannot be utilized properly by the cells and
accumulates in the blood. Fatty acid metabolism is also upset.
- hyperinsulinism (too much insulin) leads to the hypoglycemic condition. Excessive amounts of glucose
are removed from the blood. Severe hypoglycemia may result when a diabetic injects too much insulin.
A severe insulin shock may result in a coma since glucose does not reach the brain. A diabetic usually
carries a glucose rich food, such as candy, to provide a quick supply of glucose to replenish depleted
glucose levels caused by too much insulin.
- a functional type of hypoglycemia results in some individuals from an over stimulation of insulin. The
causes of hypoglycemia are not completely understood, but it occurs in some people after eating
heavily sugared food such as heavily sugared cereal and/or coffee and sweet rolls. The initial high
glucose levels over stimulates the pancreas to produce too much insulin. The excess insulin causes
blood sugar levels to drop below normal after 2-3 hours which may cause the person to feel sleepy,
irritable, and generally tired. The condition is only exacerbated by a "quick fix" of more sweetened
coffee, pastry, or candy since more insulin is produced again. A protein rich breakfast would correct
the condition by allowing glucose to enter the blood stream more slowly.
2) Glucagon – also in the pancreas and functions to raise blood-sugar level by activating the enzymes
(phosphorylase) which is concerned with the breakdown of glycogen to glucose
- released from the pancreas in response to low blood glucose
- increases glucose levels in the blood by stimulating the breakdown of glycogen (glycogenolysis) in the
liver into glucose which leaves the liver cells and enters the blood stream.
3) Epinephrine, or adrenaline – released by the adrenal glands in response to stress (the fight-or-flight
response: anger, fear or excitement); its main target is muscle cells, where energy is needed for quick
action; increases heart rate and blood pressure
There are six major metabolic pathways of glucose:

1) glycogenesis 4) glycolysis
2) glycogenolysis 5) hexose monophosphate shunt
3) gluconeogenesis 6) TCA cycle
The goal of glycolysis, glycogenolysis, and the citric acid cycle is to conserve energy as ATP from the catabolism of
carbohydrates. If the cells have sufficient supplies of ATP, then these pathways and cycles are inhibited. Under
these conditions of excess ATP, the liver will attempt to convert a variety of excess molecules into glucose
(gluconeogenesis) and/or glycogen (glycogenesis).
GLYCOGENESIS & GLYCOGENOLYSIS

- involved in the regulation of glucose concentration
- when the dietary intake of glucose exceeds immediate needs, humans and other animals can convert
the excess to glycogen, which is stored in either the liver or muscle tissue. Glycogenesis is the pathway
that converts glucose into glycogen.
- when there’s need for additional blood glucose, glycogen is hydrolyzed and released into the
bloodstream. Glycogenolysis is the pathway that hydrolyzes glycogen to glucose.
- when intake of glucose exceeds immediate needs and the capacity to store glycogen, the excess can be
converted into fat which can be stored in unlimited quantities
2
GLUCONEOGENESIS
- the total supply of glucose (blood glucose; liver & muscle glycogen) can be depleted after about 12-18
hours of fasting. Between meals, the liver begins to draw on the fats and proteins of tissues for the
building blocks from which to synthesize the required glucose.
- Gluconeogenesis is the process of synthesizing glucose from non-carbohydrate sources.
- similar but not the exact reverse of glycolysis.
- the starting point of gluconeogenesis is pyruvic acid, although oxaloacetic acid and dihydroxyacetone
phosphate also provide entry points. Lactic acid, some amino acids from protein and glycerol from fat
can also be converted into glucose.
- Notice that oxaloacetic acid is synthesized from pyruvic acid in the first step. Oxaloacetic acid is also
the first compound to react with acetyl CoA in the citric acid cycle. The concentration of acetyl CoA
and ATP determines the fate of oxaloacetic acid. If the concentration of acetyl CoA is low and
concentration of ATP is high then gluconeogenesis proceeds. Also notice that ATP is required for a
biosynthesis sequence of gluconeogenesis.
- Gluconeogenesis occurs mainly in the liver with a small amount also occurring in the cortex of the
kidney. Very little gluconeogenesis occurs in the brain, skeletal muscles, heart muscles or other body
tissue. In fact, these organs have a high demand for glucose. Therefore, gluconeogenesis is constantly
occurring in the liver to maintain the glucose level in the blood to meet these demands.
HEXOSE MONOPHOSPHATE SHUNT (HMP Shunt)

- name is derived from the initial reactant of this pathway: glu-6-P
- also termed phosphogluconate pathway, because 6-phosphogluconate is one of the intermediates
- a third name is pentose-phosphate pathway, because ribose-5-P is one of its products
- the main purposes of the HMP shunt are the following:
o to produce ribose-5-P for nucleotide
synthesis
o to produce NADPH from NADP+
for fatty acid and steroid biosynthesis
and for maintaining reduced glutathione
(GSH) inside erythrocytes
o to interconvert pentoses and hexoses
3
GLYCOLYSIS
- a series of reactions in the cytoplasm that converts the 6-carbon glucose molecule into two 3-carbon
pyruvate fragments for entry into the Krebs cycle in the mitochondria
- also called Embden-Meyerhof Pathway, after the scientists who elucidated the degradation of glucose
and glycogen in the absence of O 2
- an anaerobic process; each step takes place without O 2 ; one of its advantages, the body can obtain
energy from glycolysis quickly, without waiting for a supply of O 2 to be carried to the cells.
- occurs in cells lacking mitochondria, e.g., erythrocytes and in certain skeletal muscle cells during
intense muscle activity
- produces a net gain of 2 ATP by a process called substrate-level phosphorylation.
4
Reaction 1
• substrate glucose is phosphorylated by hexokinase to form glucose-6-phosphate at the expense of ATP
• expenditure of ATP early in the pathway works as energy “debt” necessary to get the pathway started
Reaction 2
• glucose-6-phosphate is rearranged to the structural isomer fructose-6-phosphate by enzyme phosphogluco
isomerase; product has an “exposed” C-1, no longer part of the ring structure; converts an aldose to a
ketose
Reaction 3
• substrate fructose-6-phosphate is phosphorylated by phosphofructokinase to fructose-1,6-bisphosphate
• again the expenditure of ATP early in the pathway works as energy “debt” necessary to get the pathway
started
Reaction 4
• fructose-1,6-bisphosphate is split into two 3-carbon intermediates by the enzyme aldolase forming
dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-phosphate (G3P)
Reaction 4A
• DHAP is rearranged into a second G3P by triose phosphate isomerase; G3P is the only substrate for the
next reaction
Reaction 5
• G3P is oxidized to a carboxylic acid by G3P dehydrogenase; oa is NAD+; transfers an inorganic phosphate
group to the carboxyl group to form 1,3-bisphosphoglycerate
• new phosphate group attached with a “high-energy” bond; this and all subsequent steps occur twice for
each G3P
• first redox reaction in the glycolytic sequence; first step in glycolysis to “harvest” energy
Reaction 6
• 1,3-Bisphosphoglycerate high energy phosphate group is transferred to ADP by phosphoglycerate kinase
to form ATP
• harvest energy in the form of ATP; this is the first substrate level phosphorylation of glycolysis
Reaction 7
• 3-PG is isomerized into 2-PG by the enzyme phosphoglycerate mutase; new positioning is necessary for
enzyme action
Reaction 8
• enzyme enolase catalyzes dehydration of 2-PG to energy-rich phosphorylated phosphoenol pyruvate (PEP).
5
Reaction 9
• final substrate-level phosphorylation in the pathway
• phosphoenolpyruvate serves as donor of the phosphoryl group transferred to ADP by pyruvate kinase
making ATP; a coupled reaction in which hydrolysis of the phosphoester bond provides energy for the
formation of the phosphoanhydride bond of ATP
• from glycolysis pyruvate remains for further degradation and NADH must be reoxidized
• At this point of carbohydrate metabolism there are at least 2 directions that the product pyruvate may take.
The direction depends primarily upon the availability of oxygen in the cell:
a) If there is adequate oxygen, an aerobic pathway is followed and pyruvate enters the Krebs cycle.
b) If there is insufficient oxygen available, an anaerobic pathway is followed and pyruvate undergoes a
series of reactions to produce lactic acid.
Lactic acid then is the end-product of glycolysis, and if there were not some mechanism for its
removal, it would accumulate in the muscle cells.
• Lactate fermentation is the anaerobic metabolism that occurs in exercising muscle
• Bacteria also use lactate fermentation in the production of yogurt and cheese
• This reaction produces NAD+ and degrades pyruvate
Reactions 1  9 are identical for glycolysis and alocoholic fermentation
• for pyruvic acid, the crossroads compound, its metabolic fate depends upon the conditions (aerobic or
anaerobic) and upon the organism under consideration.
• Yeast ferment sugars of fruit and grains anaerobically, using pyruvate from glycolysis
• Pyruvate decarboxylase removes CO 2 from the pyruvate producing acetaldehyde
• Alcohol dehydrogenase catalyzes reduction of acetaldehyde to ethanol, releasing NAD in the process
• Pyruvate is most commonly metabolized in one of three ways, depending on the type of organism and the
presence or absence of O 2
aerobi c condi ti ons

3 CO 2 + 2 H2 O
pl ants and ani mal s
O OH
anaerobi c condi ti ons
CH3 CCOO - CH3 CHCOO-
contracti ng muscl e
Pyr uvate Lactate
anaerobi c condi ti ons
CH3 CH2 OH + CO 2
fermentati on i n yeast
Ethanol
6
TRICARBOXYLIC ACID (TCA) CYCLE
- also called KREBS CYCLE or CITRIC ACID CYCLE
- aerobic metabolism; a series of reactions taking place in the mitochondria where acetyl CoA is
oxidized to CO 2 & H 2 O
- as in other metabolic pathways, all reactions of the TCA cycle are catalyzed by enzymes; some of the
necessary enzymes are located in the fluid contained in the mitochondrial inner membrane; others are
attached to the inner surface of the interior membrane
- as we go through the steps of the cycle, be especially alert to the fates of the carbons of the reacting
molecules, the various types of transformations which are occurring, and the production of NADH,
FADH 2 , and ATP.
The Krebs Cycle is important for several reasons:

1) Not only is the Krebs Cycle the final pathway for the oxidation of carbohydrates, but it is the common
pathway for the oxidation of lipids and proteins since fatty acids and many amino acids are also
metabolized to acetyl CoA.
2) The Krebs Cycle is the mechanism that provides much of the free energy liberated during respiration.
During the course of the oxidation of acetyl CoA, hydrogen and electrons (reducing equivalents) were
formed. These reducing equivalents enter the respiratory chain where high-energy phosphates are
produced in the process of oxidative phosphorylation.
(Substrate level phosphorylation – when ATP is produced as a result of direct transfer of a phosphate
group from a metabolite to ADP.)
3) The cycle is also anabolic in function. Not only does it degrade acetyl CoA into CO 2 , but it also serves as a
source of molecules for fatty acid synthesis, amino acid synthesis, and gluconeogenesis. The TCA cycle
provides intermediates for numerous biosynthetic processes in the cell.
7
Reaction a
• pyruvic acid  acetyl CoA
• pyruvic acid cannot directly enter the Krebs Cycle; it must first be oxidized (decarboxylated) and added to
CoA
• involves oxidative decarboxylation of pyruvic acid to yield the important intermediate acetyl CoA
• the process is irreversible and requires the participation of five cofactors: CoASH, thiamine pyrophosphate
(TPP), lipoic acid, NAD+, and Mg2+; and the enzyme pyruvic acid oxidase.
Reaction 1 aldol condensation
• acetyl CoA + oxaloacetic acid citric acid
• the early discovery of citric acid is the reason the pathway is called citric acid cycle; note that this step
regenerates CoASH
Reaction 2 -HOH +HOH
• citric acid aconitic acid isocitric acid

• the single enzyme aconitase catalyzes the successive elimination & reincorporation of a molecule of water
with a net result of isomerization of citric to isocitric acid
Reactions 3
• isocitric acid  oxalosuccinic acid  α-ketoglutaric acid
• oxidative decarboxylation of isocitric acid to α-ketoglutaric acid; usually discussed together because
experimental evidence indicates that the intermediate, oxalosuccinic acid does not exist free but is firmly
bound to the surface of the enzyme collectively called isocitric dehydrogenase
Reaction 4
• α-ketoglutaric acid  succinyl CoA
• practically identical to Reaction a requiring the same 5 cofactors
8
• the only nonreversible reaction in the Krebs Cycle and, as such, prevents the cycle from operating in the
reverse direction
Reaction 5
• succinyl CoA  succinic acid
• process requires the participation of the cofactor GDP. GTP can react with ADP to generate ATP; the step
regenerates CoASH
Reaction 6
• succinic acid  fumaric acid
• the only step in the cycle catalyzed by the coenzyme FAD, not by NAD+; involves dehydrogenation of
succinic acid
Reaction 7
• fumaric acid  malic acid
• the step involves the addition of a molecule of water across the double bond of fumaric acid to form malic
acid; step is catalyzed by fumarase, which is highly stereospecific, producing only L-malic acid
Reaction 8
• malic acid  oxaloacetic acid
• the step involves the dehydrogenation of L-malic acid to oxaloacetic acid by the enzyme malate
dehydrogenase signifying the completion of the cycle.
Summary of the TCA Cycle:

Acetyl CoA + 3NAD+ + FAD + GDP + P i + 2H 2 O  2CO 2 + CoASH + 3NADH + 2H+ + FADH 2 + GTP
Important features of the cycle:

1. The reactions of the cycle takes place in the mitochondrial matrix, except the succinate dehydrogenase
reaction that involves FAD. The enzyme that catalyzes this reaction is an integral part of the inner
mitochondrial membrane.
2. The “fuel “ for the cycle is acetyl CoA, obtained from the breakdown of carbohydrates, fats, and proteins.
3. Four of the cycle reactions involve oxidation and reduction. The oxidizing agent is either NAD+ (three
times) or FAD (once). The operation of the cycle depends on the availability of these oxidizing agents.
4. In redox reactions, NAD+ is the oxidizing agent when a carbon-oxygen double bond is formed; FAD is the
oxidizing agent when a carbon-carbon double bond is formed.
5. The three NADH and the one FADH 2 that are formed during the cycle carry electrons and H+ to the
electron transport chain through which ATP is synthesized.
6. Two carbon atoms enter the cycle as acetyl unit of the acetyl CoA, and two carbon atoms leave the cycle as
two molecules of CO 2 . The carbon atoms that enter and leave are not the same ones. The carbon atoms that
leave during one turn of the cycle are carbon atoms that entered during the previous turn of the cycle.
7. Four B vitamins are necessary for the proper functioning of the cycle: riboflavin (in both FAD and α-
ketoglutarate dehydrogenase complex), nicotinamide (in NAD+, pantothenic acid (in CoASH), and thiamin
(in α-ketoglutarate dehydrogenase complex)
8. One high-energy GTP molecule is produced by phosphorylation.
Regulation of the TCA Cycle:

The rate at which the citric acid cycle operates is controlled by the body’s need for energy (ATP). When
the body’s ATP supply is high, the ATP present inhibits the activity of citrate synthase, the enzyme in reaction 1 of
the cycle. When energy is being used at a high rate, a state of low ATP and high ADP concentrations, the ADP
activates citrate synthase and the cycle speeds up. A similar control mechanism exists at reaction 4 which involves
isocitrate dehydrogenase; here NADH acts as an inhibitor and ADP as an activator.
RESPIRATORY CHAIN AND ELECTRON TRANSPORT SYSTEM

• the series of reactions that move H+ and electrons (reducing equivalents) along a series of carriers in the
mitochondria
• the sequence of reactions whereby the reduced forms of the coenzymes are reoxidized, ultimately by O 2
• ultimately results in the production of energy and water
• for each molecule of pyruvic acid that is converted to CO 2 and H 2 O via the Krebs cycle, five
dehydrogenation steps occur (reactions a, 3,4,6 & 8)
9
• SH 2 symbolizes the reduced metabolites (i.e., pyruvic acid, isocitric acid, α-ketoglutaric acid, and malic
acid) and S signifies the oxidized metabolites (i.e., acetyl CoA, oxalosuccinic acid, succinyl CoA, and
oxaloacetic acid)
ATP 2H+ ADP + P i ATP
SH 2 NAD+ FADH 2 Quinone 2Fe2+ 2Fe3+ 2Fe2+ 2Fe3+ HOH
Coenzyme Q 10 cyt b cyt c cyt a cyt a 3
S NADH FAD Hydroquinone 2Fe3+ 2Fe2+ 2Fe3+ 2Fe2+ ½ O2
H+ H+ 2H+
ADP + P i ATP ADP + P i
OXIDATIVE PHOSPHORYLATION
• the process whereby ATP is synthesized as a result of the operation of the respiratory chain is referred to as
oxidative phosphorylation
• the details of the mechanism which links the formation of ATP to the operation of the respiratory chain is
largely unknown. It is known, however, that the energy required for the production of ATP results from the
passage of a pair of electrons from one carrier to the next.
• the electron transport system can be thought to function as a biochemical battery; that is, energy is obtained
from oxidation-reduction reactions
The maximum amount of energy that is made available when a single pair of electrons travel from NADH to O 2
along the chain:
E’ (volts)
NADH  NAD+ + H+ + 2e- +0.32 The free energy for the reaction, ∆G’ = -nFE
½ O 2 + 2H+ + 2e-  H 2 O +0.82 ∆G’ = -
(2)(23,000)(1.14)
--------------------------------------------------------------------------
NADH + ½ O 2 + H+  NAD+ + H 2 O +1.14 ∆G’ = -52,000 cal
• this value of 52,000 calories represents a considerable amount of energy. If it were released all at once,
much of it would be dissipated as heat and it might prove damaging to the cell. The respiratory chain serves
as a device for delivering this energy in small increments to be used to phosphorylate ADP.
• it has been experimentally observed that three (3) molecules of ATP are formed for every molecule of
NADH that is oxidized in the chain but only two (2) ATPs are formed if the primary acceptor is FAD, as in
the case when succinic acid serves as a substrate.
• almost half of the energy released in the electron transport process is conserved in the formation of high-
energy phosphate bonds.
The net equation for the respiratory chain is:

NADH + ½ O 2 + H+ + 3ADP + 3P i  NAD+ + H 2 O + 3ATP
10
Energy yield of complete GLUCOSE oxidation to CO 2 and H 2 O
Type of No. of ATP
Reaction phosphorylation formed
Glucose  2 pyruvic acid Substrate level 2

NAD+ NADH + H+
Oxidative 2 x 3
Glyceraldehyde-3-phosphate 1,3-diphosphoglyceric
acid
NAD+ NADH + H+
Oxidative 2 x 3
Pyruvic acid Acetyl CoA
NAD+ NADH + H+
Oxidative 2 x 3
Isocitric acid Oxalosuccinic acid
NAD+ NADH + H+
Oxidative 2 x 3
α-ketoglutaric acid Succinyl CoA
GDP GTP
Substrate level 2 x 1
Succinyl CoA Succinic acid
FAD FADH 2
Oxidative 2 x 2
Succinic acid Fumaric acid
NAD+ NADH + H+
Oxidative 2 x 3
Malic acid Oxaloacetic acid
TOTAL = 38
The net equation for the oxidation of glucose:

C 6 H 12 O 6 + 6O 2 + 38ADP + 38P i  6CO 2 + 6H 2 O + 38ATP
11
12
13
V. ENZYMES
ENZYMES are the biological catalysts produced by living cells. Each cell in the human body contains thousands
of different enzymes, because almost every reaction in a cell requires its own specific enzyme. Enzymes cause
cellular reactions to occur millions of times faster than corresponding uncatalyzed reactions. An enzyme speeds a
reaction by lowering the activation energy, changing the reaction pathway. This provides a lower energy route for
conversion of substrate to product.
As catalysts, enzymes are not consumed during the reaction but merely help the reaction occur more rapidly. If
there are no enzymes, most reactions occurring in the body would be so slow that they would not be able to
support life.
Composition of enzymes:
- Most enzymes are globular proteins; some are simple proteins, others are conjugated proteins
- Until the 1980’s it was thought that all enzymes were proteins, a few enzymes are now known that are made
of ribonucleic acids and catalyze cellular reactions involving nucleic acids.
1) simple proteins
- consist entirely of amino acid units; it is the 3o structure of the simple proteins (enzymes) that makes it
biologically active; eg, pepsin, trypsin, ribonuclease, etc.
2) conjugated proteins
a) apoenzyme  protein part; inactive in itself
b) coenzyme (cofactor)  nonprotein organic moiety; the activator; loosely bound to protein; called
prosthetic group if coenzyme/cofactor is permanently bound
a metallic ion (Fe2+ ; Mg+ ; Co2+ ; Zn2+, Mn2+, etc)
HOLOENZYME  the resulting complete, active enzyme when the apoenzyme has been activated by
the coenzyme
Nomenclature of enzymes:
Enzymes are most commonly named by using a system that attempts to provide information about the
function (rather than the structure) of the enzyme. Type of reaction catalyzed and substrate identity are focal
points for the nomenclature. A substrate is the reactant in an enzyme-catalyzed reaction - the substance upon
which the enzyme “acts”. Important aspects in naming enzymes are as follows:
1. The suffix –ase identifies a substance as an enzyme; e.g., urease, sucrase, lipase are all enzyme designations.
The suffix –in is still found in many of the digestive enzymes; e.g., trypsin, pepsin
2. The type of reaction catalyzed by an enzyme is often noted with a prefix; e.g., oxidase catalyzes oxidation
reaction, hydrolase catalyzes hydrolysis reaction.
1
3. The identity of the substrate is often noted in addition to the type of reaction; e.g., glucose oxidase, pyruvate
carboxylase, succinate dehydrogenase.
4. Infrequently, the substrate but not the reaction type is given; urease, lactase.
Classification of enzymes:
To systematize the nomenclature for enzymes the International Union of Biochemists has grouped
enzymes into six major classes
1. Oxidoreductases - catalyze oxidation-reduction involving substrate molecules
a. Oxidases – oxidation of a substrate
b. Reductases – reduction of a substrate
c. Dehydrogenase – introduction of a double bond (oxidation) by formal removal of H2 from
substrate, the hydrogen being accepted by a coenzyme
2. Transferases - catalyze transfer of functional groups between two substrates

a. Kinases – transfer of a phosphate group between substrates
b. Transaminase – transfer of an amino group between substrates
3. Hydrolases - catalyze the addition of a water molecule to a bond causing the bond to break
a. Proteases – hydrolysis of peptide linkages in proteins
b. Carbohydrases – hydrolysis of glycosidic bonds in carbohydrates: sucrase, lactase, cellulase

c. Lipases – hydrolysis of ester linkages in lipids
2
d. Nucleases – hydrolysis of sugar phosphate ester bonds in nucleic acids
e. Phosphatases – hydrolysis of phosphate ester bonds
4. Lyases - catalyze the addition of a group to a double bond or the removal of a group to create a
double bond in a manner that does not involve hydrolysis
a. Dehydratases – removal of water from substrate
b. Decarboxylases – removal of carbon dioxide from substrate
c. Deaminases – removal of ammonia from substrate
5. Isomerases - catalyze the conversion of a substrate into another compound that is isomeric with it
a. Racemases – conversion of D to L isomer or vice versa
b. Mutases – transfer of a functional group within a molecule
3
c. Epimerases – conversion of one sugar epimer into another
6. Ligases - catalyze the bonding together of two substrate molecule with participation of ATP
a. Synthetases – formation of new bond between two substrates with participation of ATP
b. Carboxylases – formation of new bond between substrate and carbon dioxide with
participation of ATP
The Models of Enzyme Action

Explanations of how enzymes function as catalysts in biochemical systems are based on the concepts of
an enzyme active site and enzyme-substrate complex formation.
4
Enzyme active site
It is the relatively small part of an enzyme that is actually involved in catalysis; a small portion of an
enzyme surface where the substrate(s) becomes bound by noncovalent forces, e.g., hydrogen bonding, electrostatic
attractions, van der Waals attractions. It is a three-dimensional entity formed by groups that come from different
parts of the protein chain(s); these groups are brought together by the folding and bending (2o & 3o structure) of
the protein. The active site is usually a “crevice-like” location in the enzyme.
Enzyme-substrate complex
Catalysts offer an alternative pathway with lower activation energy through which a reaction can occur.
In enzyme-controlled reactions, this alternative pathway involves the formation of an enzyme-substrate complex
as an intermediate species in the reaction. An enzyme-substrate complex is the intermediate reaction species that is
formed when a substrate binds to the active site of an enzyme. Within the enzyme-substrate complex, proximity
effects and orientation effects create more favorable reaction conditions than if substrates were free. The result is
faster formation of products.
The forces that draw the substrate into the active site are many of the same forces that maintain tertiary structure
in the folding of the polypeptide chains. Electrostatic interactions, hydrogen bonds, and hydrophobic interactions
all help attract and bind substrate molecules. For example, a protonated (positively charged) amino group in a
substrate could be attracted and held at the active site by a negatively charged aspartate or glutamate residue.
Alternatively, cofactors such as positively charged metal ions often help bind substrate molecules.
Lock-and-Key model
Just as the notches on a key are designed to fit a specific lock, active sites on a protein are designed to fit a
specific substrate. In this model, the active site in the enzyme has a fixed, rigid geometrical conformation. Only
substrates with a complementary geometry can be accommodated at such site, much as a lock accepts only certain
keys. This model fails to take into account proteins’ conformational changes to accommodate a substrate molecule
Induced-Fit model
The induced-fit model of enzyme action assumes that the enzyme active site is a more flexible pocket whose
conformation changes to accommodate the substrate molecule. It allows for small changes in the shape or
geometry of the active site of an enzyme in order to accommodate a substrate. This is a more thorough explanation
for the active-site properties of an enzyme because it includes the specificity of the lock-and-key model coupled
with the flexibility of the enzyme protein
5
Specificity of Enzymes
1) Absolute specificity
- catalyze a particular reaction for one particular substrate only and will have no catalytic effect on substrates
which are closely related
- eg, urease  acts only on urea H2N – CO – NH2
not for methylurea H2N – CO – NHCH3
nor biuret H2N – CO – NH – CO – NH2
2) Stereochemical specificity
- catalyze a specific stereochemical representation
- eg. acid dehydrogenase catalyzes the oxidation of L-lactic acid (in muscle tissues) but not D-lactic acid (in
microorganisms)
3) Group specificity
- less selective and will act upon structurally similar molecules
- eg, carboxypeptidase catalyzes the hydrolysis of C-terminal groups regardless of what amino acid
4) Linkage specificity
- the least specific; attack a particular kind of chemical bond, irrespective of the structural features in the
vicinity of the linkage
- eg, lipase catalyzes the hydrolysis of any kind of ester
Factors Affecting Enzyme Activity

Enzyme activity is a measure of the rate at which an enzyme converts substrate to products. Four factors
affect enzyme activity: substrate concentration, enzyme concentration, temperature, & pH.
1) Concentration of substrate
- enzyme activity increases proportionally with [S] until a limiting rate is reached (when all enzyme surface
has been used for reaction).
- enzyme activity increases up to a certain substrate concentration and thereafter remains constant – this
activity pattern is called a saturation curve.
- as substrate concentration increases, the point is eventually reached where enzyme capabilities are used to
their maximum extent, the rate remains constant from this point on. Each substrate must occupy an enzyme
active site for a finite amount of time, and the products must leave the site before the cycle can be repeated.
When each enzyme molecule is working at full capacity, the incoming substrate molecules must “wait their
turn” for an empty active site. At this point, the enzyme is said to be under saturating conditions.
6
- the rate at which an enzyme accepts and releases substrate molecules at substrate saturation is given by its
turnover number, which is equal to the number of substrate molecules transformed per second by one
molecule of enzyme under optimum conditions of temperature, pH, and saturation; some enzymes have a
much faster mode of operation than others; e.g., carbonic anhydrase (600,000), glutamate dehydrogenase
(500), phosphoglucomutase (21), chymotrypsin (2)
2) Concentration of the enzyme

- If the amount of substrate present is kept constant and the enzyme concentration is increased, the reaction rate
increases because more substrate molecules can be accommodated in a given amount of time; enzyme
activity increases proportionally with [E]
3) Temperature
- Temperature is a measure of the kinetic energy (energy of motion) of molecules; higher temperatures mean
molecules are moving faster and colliding more frequently.
- As the temperature of an enzymatically catalyzed reaction increases, so does the rate of the reaction. When
the temperature increases beyond a certain point, however, the increased energy begins to cause disruptions
in the tertiary structure of the enzyme; denaturation is occurring. Tertiary structure change at the active site
impedes catalytic action, and the enzyme activity quickly decreases as the temperature climbs past this point.
The temperature that produces maximum activity for an enzyme is known as the optimum temperature for
that enzyme; for human enzymes, the optimum temperature is often 37oC, normal body temperature.
4) pH
- The pH of an enzyme’s environment can affect its activity because the charge on acidic and basic amino
acids located at the active site depends on pH; small changes in pH (less than one unit) can result in enzyme
denaturation and subsequent loss of catalytic activity.
- Most enzymes exhibit maximum activity over a very narrow pH range; only within this narrow pH range do
the enzyme’s amino acids exist in properly charged forms
- Optimum pH is the pH at which an enzyme has maximum activity; biochemical buffers help maintain the
optimum pH for an enzyme
- Each enzyme has a characteristic optimum pH, which usually falls within the physiological pH range of 7.0-
7.5 , except digestive enzymes pepsin (functions best at pH 2.0) and trypsin (functions best at pH 8.0)
- A variation from normal pH can also affect substrates, causing either protonation or deprotonation of groups
on the substrate. The interaction between the altered substrate and the enzyme active site may be less efficient
than normal – or even impossible.
7
Regulation of Enzyme Activity
Enzyme activity is often regulated by the cell to conserve energy. If the cell runs out of chemical energy, it will die;
therefore many mechanisms exist to conserve cellular energy.
1. Produce the enzyme only when the substrate is present – the simplest mechanism
2. Allosteric enzymes – effector molecules change the activity of an enzyme by binding at a second site
a) active site or catalytic site - where the substrate binds lock-and-key
b) allosteric site (meaning “another site”) - where the effector/inhibitor binds; distorts active site
• some effectors speed up enzyme action (positive allosterism)
• some effectors slow enzyme action (negative allosterism)
3. Feedback inhibition (negative feedback control) - the enzyme catalyzing the first reaction in the pathway
is inhibited by the final product which the pathway produces; an effective way of controlling the rate
of synthesis of a molecule according to the cell’s needs.
4. Production of proenzymes (zymogen) – enzyme in an inactive form; converted by proteolysis to the active
form when it has reached the site of its activity; e.g., pepsinogen H+ pepsin
5. Protein modification – another mechanism that the cell can use to turn an enzyme on or off is protein
modification where the most common is addition (phosphorylation) or removal (dephosphorylation) of a
phosphate group. For example, phosphorylation can either activate (orange) a protein or inactivate it (green).
Kinase is an enzyme that phosphorylates proteins. Phosphatase is an enzyme that dephosphorylates proteins,
effectively undoing the action of kinase.
Inhibition of Enzyme Activity

1. Irreversible inhibitors
- substances that cause inhibition that cannot be reversed; bind tightly to the enzyme and thereby prevent
formation of the E-S complex; covalently or noncavalently bound to the target enzyme and dissociates very
slowly from the enzyme; e.g., diisopropylphosphofluoridate (DIPF) and iodoacetamide.
8
2. Reversible inhibitors - substances that bind to an enzyme to inhibit it, but can be released
Competitive inhibition
- any compound which bears a close structural resemblance to a particular substrate and which competes with
that substrate for the same active sites on the enzyme is said to be a competitive enzyme inhibitor
- in competitive inhibition, a substrate and an inhibitor compete for the active sites on the enzyme. They are so
similar in structure that the enzyme binds to the inhibitor by mistake. As long as the competitive inhibitor
occupies the active site, no reaction of the substrate can take place. However, competitive inhibition may be
reversed by adding more substrate that competes with the inhibitor for the active site
- competitive enzyme inhibitors are also called structural analogs
Noncompetitive inhibition
- this type of inhibition involves inhibitors that can bind at sites different from the active sites of the enzyme;
these inhibitors do not interfere with the binding of the substrate to the enzyme directly but interfere with the
reaction of the enzyme-substrate complex.
- occur when a foreign substance (inhibitor) attaches to only a portion of the enzyme tying up one or two active
sites , or if a bulky foreign substance blocks the entrance of the substrate to the enzyme
Chemotherapy
- refers to the use of chemicals to destroy infectious microorganisms without damaging the cells of the host
A. Antimetabolites (act through competitive inhibition)
- eg. Inhibition by a Sulfa drug : Sulfa drugs are similar to PABA, a compound that bacteria must have to
synthesize folic acid. Sulfa drugs react with the enzymes that usually complex with PABA, preventing them
from forming folic acid. Humans get their folic acid preformed from foods, not synthesized by our system
9
B. Antibiotics
- bacteria have one structural feature not found in animal cells – a cell wall. Penicillin acts by complexing with
the enzymes responsible for cell wall synthesis, effectively killing the bacteria. Since animal cells do not have
cell walls, there are no such enzymes to be affected and penicillin has no effect on animal cells.
- the bacterial cell wall precursor is a polymer comprising a repeating disaccharide unit with attached
polypeptide side chains that end with a d-alanyl-d-alanine unit. The transpeptidase enzyme cleaves the
terminal d-alanine and the amino group of the glycine then reacts with the penultimate d-alanine on a
neighbouring chain to produce the mature cross-linked matrix of the cell wal. The structural similarity
between the penicillins and d-alanyl-d-alanine allows the antibiotics to act as inhibitory substrates for the
transpeptidase enzyme.
Michaelis – Menten Kinetics of Enzyme Action

k1 k3
For a monosubstrate reaction: E + S ↔ ES ↔ E + P
k2 k4
if k3 is very small, initial velocity, υ = k3 ES
when substrate concentration is very high vmax = k3 ET (ET = total E ; free + bound E)
Rate of formation of ES = dES/dt = k1 (E – ES) (S)
Rate of breakdown of ES = - dES/dt = k2 (ES) + k3 (ES)
At steady state, with [ES] remaining constant, where there is a dynamic steady state with substrates continually supplied
and products continually removed removed as in the usual situation in the living cell
k1 (E – ES) (S) = k2 (ES) + k3 (ES)
(E - ES) (S) / (ES) = k2 + k3 / k1 = Km (Michaelis constant)
to solve for ES:
(E - ES) (S) / (ES) = Km
(E)(S) / (ES) - (ES)(S) / (ES) = Km
(E) (S) / (ES) = Km + (S)
(ES) = (E) (S) / Km + (S)
if υ = k3 ES and vmax = k3 E
υ = k3 (E) (S) / Km + (S)
= vmax / (E) . (E) (S) / Km + (S)
υ = (vmax) (S) / Km + (S) → Michaelis Equation (Fig. 6.4 - p126 McKee)
where υ = observed initial velocity of the reaction
(S) = substrate concentration
Km = Michaelis constant
vmax = maximum velocity of enzyme reaction
The equation states that, when the [S] is very high, Km is negligible compared to the [S] and the equation
reduces to υ = vmax , that is , the observed velocity is maximal at high [S]. Conversely, when [S] is very low,
then Km + (S) becomes appreciable compared to (S) and the observed velocity, υ, is a fraction of the vmax ;
υ = (S) / Km + (S) · vmax

when υ = ½ vmax
vmax / 2 = vmax (S) / Km + (S) ; dividing both sides by vmax
½ = (S) / Km + (S)
Km + (S) = 2 (S)
Km = (S)
Km is equal to substrate concentration if υ = ½ vmax
- Km is the dissociation constant for ES;
the greater the value of Km, the less tightly S is bound to E;
- there is a characteristic Km value for each enzyme
(lying bet. 10-1 - 10-6 ) expressed in moles of substrate per liter
- Vmax is the turnover number
10
Lineweaver – Burke Plots
- an alternative linear transformation of the M-M equation
- estimation of the value of Km is inconvenient from Michaelis Equation plot and several more convenient forms
of the equation have been developed. The reciprocal of the equation, a linear form called the Lineweaver – Burke
plot is used.
1/υ = Km + (S) / vmax (S) = Km / vmax (S) + (S) / vmax (S) = Km / vmax x 1 / (S) + 1 / vmax (eqn for st. line)
As shown in the figure, if one plots 1/υ vs. 1/(S), the slope of the line is Km/vmax & the intercept on the ordinate
is 1/vmax..Since vmax can be obtained from the intercept it is possible to calculate Km.The intercept on the abscissa
is equal to – 1/ Km
11
Coenzymes
- the water-soluble vitamins, which include all B-vitamins and Vitamin C, act as coenzymes or coenzyme
precursors
Vitamin Coenzyme Function Deficiency Symptoms

1) Thiamine (B1) Thiamine Decarboxylation of α-keto beriberi (fatigue, anorexia,
pyrophosphate acids; cetain rexns of keto nerve degeneration, paralysis
(TPP) sugars heart failure)
2) Riboflavin (B2) Flavin mononucleotide Several kinds of redox dermatitis, glossitis (tongue
Flavin adenine reactions inflammation),cataracts
dinucleotide
(FMN, FAD)
3) Niacin/Nicotinic Nicotinamide adenine Numerous redox reactions pellagra(scaly skin, muscle

acid (B3) dinucleotide fatigue, diarrhea, mouth
Nicotinamide adenine sores, mental disorders
dinucleotide phosphate
(NAD, NADP)
4) Pantothenic acid Coenzyme A Many reactions of fatty no deficiency known, may

(B5) acids particularly those cause fatigue, anemia
involving the transfer of
acetyl groups
5) Pyridoxine (B6) Pyridoxal phosphate Several kinds of reactions dermatitis, fatigue, anemia
(PP) involving aa’s;eg, decarbo- irritability, convulsions
xylation, transamination in infants
6) Biotin Biotin CO2 fixation reactions dermatitis, fatigue, anemia

nausea, mental depression
7) Folic acid Tetrahydrofolic acid Various reactions involving abnormal rbc & wbc, gi
(THF) single C-compounds disturbances
8) Cyanocobalamine “Cobamide” Carbon chain isomerization; pernicious anemia,

coenzymes methyl group transfers (eg, malformed rbc, neurological
in rbc biosynthesis) disorders
9) Ascorbic acid (Vitamin C)

- needed for collagen formation, protein metabolism, iron absorption, healing of wounds; scurvy (bleeding
gums, slow healing wounds, muscle pain, anemia)
Role of Vit. C in collagen formation

Collagen also contains hydroxylysine and hydroxylproline. Hydroxylation of lysine and proline in
collagen formation are catalyzed by enzymes and require ascorbic acid (Vit. C). In Vit. C deficiency,
hydroxylation is impaired, and the triple helix of the collagen is not assembled properly. Persons deprived of Vit.
C develops scurvy, a disease whose symptoms include skin lesions, fragile blood vessels, loose teeth, and
bleeding gums (Voet, p 157)
12
Cofactors
=================================================================================
Metal Ion Enzymes
-----------------------------------------------------------------------------------------------------------------------------------------
Ca 2+ Thromboplastin
Cu2+ Tyrosinase, cytochrome oxidase
Fe2+ ; Fe3+ Cytochrome oxidase, catalase, dehydrogenase
Mg2+ Pyruvate kinase
Mn2+ Arginase, pyruvate carboxylase, phosphatase, succinic dehydrogenase, glycosyl transferases,
cholinesterase
K+ Pyruvate kinase
Zn2+ Carbonic anhydrase, carboxypeptidase, lactic dehydrogenase, alcohol dehydrogenase
=================================================================================
CLINICAL APPLICATIONS OF ENZYMES

Isoenzymes in Medical Diagnosis
Different cells in the body produce enzymes for the same type of reactions. Although the proteins are
similar, they are not identical. Enzymes that catalyze the same reactions but vary slightly in structure are called
isoenzymes. For example, there are five isoenzymes for lactate dehydrogenase (LDH), an enzyme that converts
lactic acid to pyruvic acid. Each LDH consists of a quaternary structure containing four subunits. In heart muscle,
the most prevalent subunit is designated as H. In skeletal muscle, the major subunit is designated as M.
Isoenzyme LDH1 LDH2 LDH3 LDH4 LDH5

Subunits H4 H3M H2M2 HM3 M4
Abundant in Heart, kidneys Heart, kidneys, Kidneys, brain Spleen Liver, skeletal
brain, rbc muscle
In healthy tissues, these enzymes are contained within cellular membranes. However, if the cells of a
particular organ are damaged, the contents including the enzymes spill into the blood. By identifying the
isoenzyme that becomes elevated in the blood serum, it is possible to determine which type of tissue has been
damaged. For example, liver diseases can be detected by a rise in the serum LDH5 level. When a myocardial
infarction (MI), or heart attack, damages the cells in the heart muscle, there is an increase in the serum LDH1
level.
13
Serum Enzymes used in diagnosis of tissue damage
Organ Condition Diagnostic Enzymes
Heart Myocardial infarction Lactate dehydrogenase (LDH1) ; Creatine kinase (CK2) ;
Glutamic oxaloacetic transaminase (GOT)
Liver Cirrhosis, carcinoma, Glutamic pyruvic transaminase (GPT) ; Lactate dehydrogenase

Hepatitis (LDH5) ; Alkaline phosphatase (ALP) ; GOT
Bone Rickets, carcinoma Alkaline phosphatase (ALP)

Pancreas Pancreatic diseases Amylase ; Cholinesterase ; Lipase (LPS)
Prostate Carcinoma Acid phosphatase (ACP)
FUNCTIONS OF ESSENTIAL ELEMENTS

ELEMENT MAJOR FUNCTIONS
Carbon Structural – in carbohydrates, lipids, proteins, and nucleic acids
Hydrogen Structural - in carbohydrates, lipids, proteins, and nucleic acids
Oxygen Structural – in carbohydrates, lipids, proteins, and nucleic acids
Nitrogen Structural – in proteins, nucleic acids, chlorophyll, certain coenzymes
Phosphorus Structural – in nucleic acids, phospholipids, ATP (energy transfer compound)
Calcium Structural – in middle lamella of cell walls
Physiological – role in membrane permeability; enzyme activation
Magnesium Structural – in chlorophyll
Physiological – enzyme activator in carbohydrate metabolism
Sulfur Structural – in certain amino acids and vitamins
Potassium Physiological – osmosis and ionic balance; opening and closing of stomata; enzyme
activator (for 40+ enzymes)
Chlorine Physiological – ionic balance; involved in light reactions (oxygen evolution) of
photosynthesis.
Iron Physiological – part of enzymes involved in photosynthesis, respiration, and nitrogen
fixation.
Manganese Physiological – part of enzymes involved in respiration and nitrogen metabolism;
required in oxygen evolution in photosynthesis
Copper Physiological – part of enzymes involved in photosynthesis
Zinc Physiological – part of enzymes involved in respiration and nitrogen metabolism
Molybdenum Physiological – part of enzymes involved in nitrogen metabolism
Boron Physiological – exact role unclear; involved in membrane transport and calcium
utilization
14
15
Proteins
Presented by:
Jhon Abrien S. Soliza, RCh
PROTEINS
• are high molar mass compounds
consisting largely or entirely of
chains of amino acids.
• They are utilized in the building of
new tissues and in the maintenance of
tissues already developed.
PROTEINS
Glycine Collagen Skin
PROTEINS
Roles
1. Mechanical Support
2. Mechanical Work
3. Catalysis
4. Transport and Storage
5. Communication and Defense
CLASSIFICATION of PROTEINS
A. Based on Composition
• Simple protiens –
• contain purely amino acid
residues
• Conjugated proteins + nonprotein
moiety(carbohydrates, lipids,
viruses, phosphate)
B. Based on structural shape
• fibrous protein
• keratin
• globular protein
• hemoglobin
C. Based on Function
C.1. Dynamic functions
• Enzymes
• catalyze chemical reactions
• Transport protiens
• myoglobin transport O2 in blood
• Transferrin transports iron from the liver to the bone marrow
• transport of TAG, cholesterol, etc.; drugs and toxic compounds
• Contractile mechanisms
(movement)
• Actin, Myosin, Tubulin
• cytoskeleton
• Protective role through a

combination
• Antibodies (IgM, IgG,
IgD, IgE and IgA)
• Regulatory function by
hormones
• Storage
• Casein, ferritin
BONDING and PROTEIN STRUCTURE
Protein synthesis
Protein synthesis
Protein synthesis GCG = ALANINE
UGC= CYSTEINE
Primary structure
• The 1o structure of a protein is the

sequence of amino acid residues in a
protein chain
• the 1o structure of proteins are
translations of information contained
in genes
Amino Acids Polymerize to Form Peptides
• Peptides bond:
– Covalent
– Formed through
condensation of amino
acids.
– Broken through
hydrolysis
Secondary Structures
• Secondary structure refers to a local spatial
arrangement of the polypeptide backbone.
• Two regular arrangements are common:
–Alpha Helix (1 polypeptide chain)
–Beta Pleated Sheet (2 or more polypeptide
chain)
The Weak Forces
• van der Waals: 0.4 - 4 kJ/mol
• hydrogen bonds: 12-30 kJ/mol
• ionic bonds: 20 kJ/mol
• hydrophobic interactions: <40 kJ/mol
the a helix
stabilized by hydrogen bonds between nearby residues
the b sheet
stabilized by hydrogen bonds between adjacent segments that may
not be nearby.
• Hydrogen bonds between strands •Hydrogen bonds between strands are

are bent (weaker). linear (stronger).
the b sheet
• Hydrogen bonds between strands •Hydrogen bonds between strands are

are bent (weaker). linear (stronger).
Tertiary Structure
• Tertiary structure refers to the overall

spatial arrangement of atoms in a protein.
• Stabilized by numerous weak interactions
between amino acid side chains
- largely hydrophobic and polar interactions
- can be stabilized by disulfide bonds
Tertiary Structure
• Two major classes:
• Globular
Water soluble
Ex: Antibodies, enzymes and
albumin
• Fibrous
Less water-soluble
Ex: Keratin (wool), collagen and
fibroin (silk fiber)
Structure of a-Keratin in Hair
Chemistry of Permanent Waving
Motifs (folds)
• Specific arrangement of several secondary

structure elements
– all a helix
– all b sheet
– both
• Motifs can be found as recurring structures in
numerous proteins.
• Globular proteins are composed of different motifs
folded together.
Motifs (folds)
Repeated Motifs Contribute to Final Fold
Myoglobin
The protein responsible for
Oxygen storage, mostly found on
muscles. It can be determined
using X-ray crystallography.
Composed of 153 Amino Acids and
its Heme group (prosthetic
group). Oxygen bonding happens
through the 5th Iron Coordination.
Denaturation of Proteins
Denaturation of Proteins
A protein’s function depends on its 3D structure.

Loss of structural integrity with accompanying loss of
activity is called denaturation.
Examples of Protein denaturants

1. Heat
2. pH
3. Chemicals
Quaternary Structure
A quaternary structure is formed by the assembly of
individual polypeptides into a larger functional cluster.
-This structure refers to the larger-scale
organization.
-This arrangement includes how elements of the
secondary structure are linked and packed
against one another.
Final level of protein structures. Refers to the
multi-subunit structure of proteins.
Subunit
Called for each chain of polypeptide.
Quaternary proteins comes in these
forms:
Dimer
Trimer
Tetramer
Oligomer
Non-covalent chain
Bonding by electrostatic forces
Hemoglobin
-a tetramer that has two sub-

units. Sub A has 141 residue while
Sub B has 146 residues.
-4 Oxygen molecules bind to
Hemoglobin.
Structure of Myoglobin
PROTEINS
Hemoglobin Binds Oxygen Cooperatively
• Hemoglobin (Hb) is a tetramer of two subunits (a2b2).
• Each subunit is similar to myoglobin.
Protein structure summary
• Primary structure à Residues of amino

acid
• Secondary structure à localized folding of
the 1 polypeptide
• Tertiary structure à complete folding of
grps of polypeptide
• quaternary structure à interaction of
subunits (mixture of grp of tertiary struture
Methemoglobinemia
Fe (II) is
converted to Fe
(III)
Methemoglobinemia
Treatment
Na Thiosulfate
Methylene Blue
Ascorbic Acid
Carbon Monoxide Poisoning
CO has 25,000
times stronger
affinity than
Oxygen
CO Poisoning
Treatment
1. Hyperbaric Oxygen
2. 100% Oxygen with
Hyperbaric Push
3. Carbon Dioxide +
Oxygen
Sickle Cell Anemia
PROTEINS
Sickle Cell Anemia
Hydroxyurea
Chaperone Proteins
Helps in the correct and timely

folding of many proteins.
HSP 70 – The chaperone protein that

helps misfolded proteins unfold and
refold, especially after a heat shock.
Prions
Misfolded proteins
that causes
misfolding of
proteins in the
brain.
Alzheimer’s
Disease
misfolding of the amyloid-β

protein may occur 15-20 years
before the first clinical
symptoms are observed.
The misfolded proteins
accumulate and form amyloid
plaques in the brain.
Protein Turnover
Process of recycling proteins into their

constituent amino acids for reuse in the cell.
Proteasomes breaks misfolded protein to its
amino acid forms
Protein Turnover
1. To eliminate misfolded or damaged proteins.

2. To regulate cell cycle.
3. To provide necessary cleavage of foreign
antigenic proteins for presentation to and
recognition by other immune system cells.
Recommended Energy Intakes per day Acceptable Macronutrient Distribution Ranges
Weight Energy Life stage/ Range (% of Energy)
Life stage/
(kg) (kcal) age group
age group Protein Total Fat Carbohydrate*
M F M F
Infants, mo Infants, mo
0-5 6.5 6.0 620 560 0-5 5 40–60 35–55
6 - 11 9.0 8.0 720 630 6 - 11 8–15 30–40 45–62
Children, yr Children, yr
1-2 12.0 11.5 1000 920 1-2 6–15 25–35 50–69
3-5 17.5 17.0 1350 1260 3 - 18 6–15 15–30 55–79
6-9 23.0 22.5 1600 1470 Adults, yr
10 - 12 33.0 36.0 2060 1980 ≥ 19 10–15 15–30 55–75
NOTE: Acceptable Macronutrient Distribution Range (AMDR) is the range
13 - 15 48.5 46.0 2700 2170
of intakes for a particular energy source (carbohydrate, protein or fat) that
16 - 18 59.0 51.5 3010 2280 is associated with reduced risk of chronic diseases while providing
Adults, yr adequate intakes of essential nutrients, expressed as a percentage of total
19 - 29 60.5 52.5 2530 1930 energy intake.
30 - 49 60.5 52.5 2420 1870 *The AMDR for carbohydrate is the percentage of total energy available
50 - 59 60.5 52.5 2420 1870 after taking into account that consumed as protein and fat, hence the wide
ranges.
60 - 69 60.5 52.5 2140 1610
≥ 70 60.5 52.5 1960 1540
Pregnant +300*
Lactating +500
*For 2nd and 3rd trimesters only
© 2015 Food and Nutrition Research Institute, Department of Science and Technology. All rights reserved.
Recommended Nutrient Intakes per day (Macronutrients)
Weight Energy Protein Essential Fatty Acids Dietary Fiber Water
Life stage/ (kg) (kcal) (g) (g) (mL)
α-Linolenic Acid Linolenic Acid
age group
M F M F M F (%E) (%E) M F
Infants, mo
0-5 6.5 6.0 620 560 9 8 0.5 4.5 - 680 560
6 - 11 9.0 8.0 720 630 17 15 0.5 4.5 - 890 630
Children, yr
1-2 12.0 11.5 1000 920 18 17 0.5 3.0 6–7 1000 920
3-5 17.5 17.0 1350 1260 22 21 0.5 2.0 8–10 1350 1260
6-9 23.0 22.5 1600 1470 30 29 0.5 2.0 11–14 1600 1470
10 - 12 33.0 36.0 2060 1980 43 46 0.5 2.0 15–17 2060 1980
13 - 15 48.5 46.0 2700 2170 62 57 0.5 2.0 18–20 2700 2170
16 - 18 59.0 51.5 3010 2280 73 61 0.5 2.0 20–23 3010 2280
Adults, yr
19 - 29 60.5 52.5 2530 1930 71 62 0.5 2.0 20–25 2530 1930
30 - 49 60.5 52.5 2420 1870 71 62 0.5 2.0 20–25 2420 1870
50 - 59 60.5 52.5 2420 1870 71 62 0.5 2.0 20–25 2420 1870
60 - 69 60.5 52.5 2140 1610 71 62 0.5 2.0 20–25 2140 1610
≥ 70 60.5 52.5 1960 1540 71 62 0.5 2.0 20–25 1960 1540
Pregnant +300* +25 +300
Lactating +500 +27 +500
*For 2nd and 3rd trimesters only
Recommended Nutrient Intakes per day (Vitamins)
Weight Vitamin Aa Vitamin Db Vitamin Ec Vitamin K Thiamin Riboflavin Niacind Vitamin B6 Vitamin B12 Folatee Vitamin C
Life stage/ (kg) (µg RE) (µg) (mg α-TE) (µg) (mg) (mg) (mg NE) (mg) (µg) (µg DFE) (mg)
age group
M F M F M F M F M F M F M F M F M F M F M F M F
Infants, mo
0-5 6.5 6.0 380 380 5 5 3 3 7 6 0.2 0.2 0.3 0.3 1 1 0.1 0.1 0.3 0.3 65 65 30 30
6 - 11 9.0 8.0 400 400 5 5 4 4 9 8 0.4 0.3 0.4 0.3 5 5 0.2 0.3 0.4 0.4 80 70 40 40
Children, yr
1-2 12.0 11.5 400 400 5 5 4 4 12 12 0.5 0.4 0.5 0.4 6 6 0.5 0.5 0.9 1.0 150 150 45 45
3-5 17.5 17.0 400 400 5 5 5 5 18 17 0.5 0.5 0.6 0.5 7 7 0.6 0.7 1.1 1.2 200 200 45 45
6-9 23.0 22.5 400 400 5 5 6 6 23 23 0.7 0.7 0.7 0.7 9 9 0.7 0.8 1.3 1.5 300 300 45 45
10 - 12 33.0 36.0 500 500 5 5 7 9 33 36 0.9 0.9 1.0 0.9 11 12 1.0 1.1 1.8 2.1 300 300 45 45
13 - 15 48.5 46.0 700 500 5 5 10 9 49 46 1.2 1.0 1.3 1.0 15 13 1.3 1.2 2.3 2.2 400 400 60 55
16 - 18 59.0 51.5 800 600 5 5 11 10 59 52 1.4 1.1 1.5 1.1 18 14 1.5 1.3 2.7 2.4 400 400 70 60
Adults, yr
19 - 29 60.5 52.5 700 600 5 5 10 10 61 53 1.2 1.1 1.3 1.1 16 14 1.3 1.3 2.4 2.4 400 400 70 60
30 - 49 60.5 52.5 700 600 5 5 10 10 61 53 1.2 1.1 1.3 1.1 16 14 1.3 1.3 2.4 2.4 400 400 70 60
50 - 59 60.5 52.5 700 600 10 10 10 10 61 53 1.2 1.1 1.3 1.1 16 14 1.7 1.6 2.4 2.4 400 400 70 60
60 - 69 60.5 52.5 700 600 15 15 10 10 61 53 1.2 1.1 1.3 1.1 16 14 1.7 1.6 2.4 2.4 400 400 70 60
≥ 70 60.5 52.5 700 600 15 15 10 10 61 53 1.2 1.1 1.3 1.1 16 14 1.7 1.6 2.4 2.4 400 400 70 60
Pregnant +300 +0 +0 +0 +0.3 +0.7 +4 +0.5 +0.2 +200 +10
Lactating +400 +0 +4 +0 +0.2 +0.6 +4 +0.6 +0.4 +150 +35
NOTE: Recommended Nutrient Intakes (RNI) are in bold font, while Adequate Intakes (AI) are in italics.
a 1 retinol equivalent (RE) = 1 µg retinol = 12 µg β-carotene or 24 µg other provitamin A carotenoids;1 µg RE = 3.33 IU vitamin A
b In the absence of adequate exposure to sunlight, as calciferol; 1 µg calciferol = 40 IU vitamin D
c 1 mg alpha-tocopherol equivalent (α-TE) = 1.49 IU natural form or 2.22 IU synthetic form
d As niacin equivalent (NE)
e 1 dietary folate equivalent (DFE) = 1 µg food folate = 0.6 µg folic acid from fortified foods or as supplement = 0.5 µg taken on an empty stomach
Recommended Nutrient Intakes per day (Minerals)
Weight Iron Zinc Selenium Iodine Calcium Magnesium Phosphorus Fluoride Electrolytes
Life stage/ (kg) (mg) (mg) (µg) (µg) (mg) (mg) (mg) (mg) Sodium Chloride Potassium
age group
M F M F M F M F M F M F M F M F M F (mg) (mg) (mg)
Infants, mo
0-5 6.5 6.0 0.4 0.4 2.1 2.1 7 6 90 90 200 200 26 26 90 90 0.01 0.01 120 180 500
6 - 11 9.0 8.0 10 9 4.2 3.7 10 9 90 90 400 400 50 50 275 275 0.5 0.4 200 300 700
Children, yr
1-2 12.0 11.5 8 8 4.1 4.0 17 16 90 90 500 500 60 60 460 460 0.6 0.6 225 350 1000
3-5 17.5 17.0 9 9 5.0 4.8 20 20 90 90 550 550 70 70 500 500 0.9 0.9 300 500 1400
6-9 23.0 22.5 10 9 5.1 5.0 20 19 120 120 700 700 90 90 500 500 1.2 1.1 400 600 1600
10 - 12 33.0 36.0 12 20 6.6 6.1 21 23 120 120 1000 1000 150 160 1250 1250 1.7 1.8 500 750 2000
13 - 15 48.5 46.0 19 (28) 9.2 7.4 30 29 150 150 1000 1000 220 210 1250 1250 2.4 2.3 500 750 2000
16 - 18 59.0 51.5 14 (28) 9.0 7.2 37 32 150 150 1000 1000 265 230 1250 1250 3.0 2.6 500 750 2000
Adults, yr
19 - 29 60.5 52.5 12 (28) 6.5 4.6 38 33 150 150 750 750 240 210 700 700 3.0 2.6 500 750 2000
30 - 49 60.5 52.5 12 (28) 6.5 4.6 38 33 150 150 750 750 240 210 700 700 3.0 2.6 500 750 2000
50 - 59 60.5 52.5 12 10 6.5 4.6 38 33 150 150 750 800 240 210 700 700 3.0 2.6 500 750 2000
60 - 69 60.5 52.5 12 10 6.5 4.6 38 33 150 150 800 800 240 210 700 700 3.0 2.6 500 750 2000
≥ 70 60.5 52.5 12 10 6.5 4.6 38 33 150 150 800 800 240 210 700 700 3.0 2.6 500 750 2000
Pregnant (+10) +5.1 +4 +100 +50 +0 +0 +0
Lactating +2 +6.7 +9 +100 +0 +50 +0 +0
NOTE: Recommended Nutrient Intakes (RNI) are in bold font, while Adequate Intakes (AI) are in italics.
( ) Requirements cannot be met by usual diet alone. Intake of iron-rich and iron-fortified foods and the use of supplements are
recommended, if necessary.
Estimated Average Requirements per day
Protein Vitamin Aa Thiamin Riboflavin Niacinb Vitamin B6 Vitamin B12 Folatec Vitamin C Iron Zinc Selenium Iodine Calcium Phosphorus
Life stage/ (g) (µg RE) (mg) (mg) (mg NE) (mg) (µg) (µg DFE) (mg) (mg) (mg) (µg) (µg) (mg) (mg)
age group
M F M F M F M F M F M F M F M F M F M F M F M F M F M F M F
Infants, mo
0-5 7 7 - - - - - - - - - - - - - - - - - - - - 5.5 5.1 - - - - - -
6 - 11 14 13 190 190 0.3 0.3 0.3 0.3 4 3 - - - - - - - - 8.4 8.4 2.8 2.5 8.2 7.3 - - - - - -
Children, yr
1-2 15 14 193 180 0.4 0.4 0.4 0.4 5 5 0.4 0.5 0.8 0.9 120 120 12 11 6.4 7.0 2.8 2.6 13.6 13.0 65 65 440 440 380 380
3-5 18 17 226 214 0.5 0.4 0.5 0.4 5 5 0.5 0.5 0.9 1.0 160 160 17 17 7.5 7.4 3.3 3.2 16.1 15.6 65 65 440 440 405 405
6-9 24 24 278 264 0.6 0.5 0.6 0.5 7 7 0.6 0.7 1.1 1.2 160 160 23 22 8.6 7.8 3.4 3.4 15.6 15.3 73 73 440 440 405 405
10 - 12 35 34 364 375 0.7 0.8 0.8 0.8 9 10 0.8 1.0 1.5 1.7 250 250 33 36 10.2 16.5 4.4 4.1 16.5 18.0 73 73 440 440 1055 1055
13 - 15 50 46 483 392 1.0 0.8 1.1 0.8 12 10 1.1 1.0 1.9 1.8 330 330 48 45 18.1 16.5 6.1 4.9 24.3 23.0 95 95 440 440 1055 1055
16 - 18 59 49 563 427 1.1 0.9 1.2 0.9 14 11 1.2 1.1 2.3 2.0 330 330 58 51 12.2 16.2 6.0 4.8 29.5 25.8 95 95 440 440 1055 1055
Adults, yr
19 - 29 57 49 499 433 1.0 0.9 1.1 0.9 12 11 1.1 1.1 2.0 2.0 320 320 60 52 10.4 26.0 4.4 3.1 30.3 26.3 95 95 600 600 580 580
30 - 49 57 49 499 433 1.0 0.9 1.1 0.9 12 11 1.1 1.1 2.0 2.0 320 320 60 52 10.4 26.0 4.4 3.1 30.3 26.3 95 95 600 600 580 580
50 - 59 57 49 499 433 1.0 0.9 1.1 0.9 12 11 1.4 1.3 2.0 2.0 320 320 60 52 10.4 26.0 4.4 3.1 30.3 26.3 95 95 600 600 580 580
60 - 69 57 49 499 433 1.0 0.9 1.1 0.9 12 11 1.4 1.3 2.0 2.0 320 320 60 52 10.4 26.0 4.4 3.1 30.3 26.3 95 95 600 600 580 580
≥ 70 57 49 499 433 1.0 0.9 1.1 0.9 12 11 1.4 1.3 2.0 2.0 320 320 60 52 10.4 26.0 4.4 3.1 30.3 26.3 95 95 600 600 580 580
Pregnant 71 - 1.2 1.4 14 1.6 2.2 520 - 30.3 - 30.3 160 - 580
Lactating 71 - 1.1 1.3 14 1.7 2.4 450 - 25.0 - 35.3 209 - 580
a 1 retinol equivalent (RE) = 1 µg retinol = 12 µg β-carotene or 24 µg other provitamin A carotenoids; 1 µg RE = 3.33 IU vitamin A
b As niacin equivalent (NE)
c 1 dietary folate equivalent (DFE) = 1 µg food folate = 0.6 µg folic acid from fortified foods or as supplement = 0.5 µg taken on an empty stomach
Tolerable Upper Intake Levels or Upper Limits per day
Life stage/ Vitamin Aa Vitamin D Vitamin Eb Niacinb Vitamin B6 Folateb Vitamin C Iron Zinc Selenium Iodine Calciumb Magnesiumb Phosphorus Fluoride
age group (µg RE) (µg) (mg α-TE) (mg NE) (mg) (µg DFE) (mg) (mg) (mg) (µg) (µg) (mg) (mg) (mg) (mg)
Infants, mo
0-5 600 25 c c c c c 40 4 45 c c c c 0.7
6 - 11 600 25 c c c c c 40 5 60 c c c c 0.9
Children, yr
1-2 600 50 200 10 30 300 400 40 7 90 200 2500 65 3000 1.3
3 600 50 200 10 30 300 400 40 7 90 200 2500 65 3000 1.3
4-5 900 50 300 15 40 400 650 40 12 150 300 2500 110 3000 2.2
6-8 900 50 300 15 40 400 650 40 12 150 300 2500 110 3000 2.2
9 1700 50 600 20 60 600 1200 40 23 280 600 2500 110 4000 10.0
10 - 12 1700 50 600 20 60 600 1200 40 23 280 600 2500 350 4000 10.0
13 1700 50 600 20 60 600 1200 40 23 280 600 2500 350 4000 10.0
14 - 15 2800 50 800 30 80 800 1800 45 34 400 900 2500 350 4000 10.0
16 - 18 2800 50 800 30 80 800 1800 45 34 400 900 2500 350 4000 10.0
Adults, yr
19 - 29 3000 50 1000d 35 100 1000 1000 45 45 400 1100 3000 350 4000 10.0
30 - 49 3000 50 1000d 35 100 1000 1000 45 45 400 1100 3000 350 4000 10.0
50 - 59 3000 50 1000d 35 100 1000 1000 45 45 400 1100 3000 350 4000 10.0
60 - 70 3000 50 1000d 35 100 1000 1000 45 45 400 1100 3000 350 4000 10.0
> 70 3000 50 1000d 35 100 1000 1000 45 45 400 1100 2700 350 3000 10.0
Pregnant/Lactating, yr
14 - 18 2800 50 800 30 80 800 1800 45 34 400 900 2500 350 e 10.0
≥ 19 3000 50 1000d 35 100 1000 2000 45 40 400 1000 2500 350 e 10.0
NOTE: Adapted from WHO/FAO Guidelines on Food Fortification with Micronutrients (WHO/FAO, 2006); however, WHO/FAO have only recommended ULs for vitamins A, niacin,
B6, C, D and E, calcium, selenium and zinc for adults. The remaining values are those recommended by IOM-FNB.
a As preformed vitamin A only; 1 µg RE = 3.33 IU vitamin A
b The ULs for vitamin E, niacin, folate and calcium apply to synthetic forms obtained from supplements and/or fortified foods; for magnesium, the UL applies to pharmacologic
agent and does not include intake from food and water.
c Not possible to establish due to lack of data of adverse effects in this age group; source of intake should be from food only to prevent high levels of intake.
d More recent evidences suggested lower ULs: <1000 mg/d α-TE (Horwitt, 2001); 300 mg/d α-TE (NHMRC, 2005; EFSA, 2006).
e
UL for phosphorus for pregnant and lactating women 14-50 years were 3,500 and 4,000 mg, respectively.
Additional Recommendations
Dietary Component Recommendation
Free sugars Limit intake to <10% of total energy in children and adultsa
Sodium Limit intake to <2 g in adultsb,d
Potassium Increase intake to 3,510 mg in adultsc,d
Sources:
a WHO Guideline on Sugars Intake for Adults and Children (2015); free sugars refer to all monosaccharides
and disaccharides added to foods and drinks by the manufacturer, cook or consumer, including sugars
naturally present in honey, syrups, fruit juices and fruit concentrates
b WHO Guideline on Sodium Intake for Adults and Children (2012)
c WHO Guideline on Potassium Intake for Adults and Children (2012)
d The recommendation for children is extrapolated from adults based on energy requirement:
Recommended Energy Intakechildren

Recommendation for children = Recommendation for adults × ( )
Recommended Energy Intakeadults

Biochem Lab Endterm Notes

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Biochem Lab Endterm Notes

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COLEGIO SAN AGUSTIN – BACOLOD BIOCHEMISTRY

College of Health and Allied Professions CHEM 2N

Primordial Soup Hypothesis (Oparin-Haldane hypothesis)

1. Formation of Organic Molecules

Miller – Urey Experiment

• Water condenses which nurtured life

Oparin – Haldane Hypothesis

Number of Atoms are balanced.

1 PARTICLE 1 PARTICLE 1 PARTICLE 1 PARTICLE

1 PARTICLE 1 PARTICLE 1 PARTICLE 1 PARTICLE

1 mole 1 mole 1 mole 1 mole

Mole = 6. 022 x 10 ^ 23 particles

Stoichiometric Equation – converts the moles of one compound to another

Molar mass = g/mol

𝑍𝑛𝑆𝑂' + 2𝑁𝑎 → 𝑁𝑎 ( 𝑆𝑂' + 𝑍𝑛

"#$% &'()* .#$% /0 .!- /0

𝑆𝑜𝑙𝑢𝑡𝑖𝑜𝑛 = 𝑆𝑜𝑙𝑢𝑡𝑒 + 𝑆𝑜𝑙𝑣𝑒𝑛𝑡

The coefficients in the balanced equation give

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• Mass Percent (m/m)

Suppose that a solution was prepared by

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• Volume Percent (v/v)

If a solution is made by taking 40mL of ethanol and

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• Mass-volume concentration (m/v)

if a solution is prepared from 10g NaCl in enough water

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© 2012 Pearson Education, Inc.

Solve The number of moles of Na2SO4 is obtained by

Converting the volume of the solution to liters:

Thus, the molarity is

Jhon Abrien S. Soliza

• Buffer range: the pH range where maximum

• If pK is 4.8 the buffering range is 3.8-5.8

• Buffer capacity: the molar amount of acid

If a small amount of hydroxide is added to an equimolar

Similarly, if acid is added, the F- reacts with it to form HF

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© 2012 Pearson Education, Inc.

pKa= -log(Ka) =4.2

pOH = 14.00 – pH = 14.00 – 9.00 = 5.00 !"# (%"&) !"(

(2.0 L)(0.18 mol NH4CI/L) = 0.36 mol NH4CI

1L+ 0.005L = 1.005L=V FINAL

A pH meter or indicators are used to

Weak acid-strong Ethanoic acid and

Strong acid-weak Hydrochloric acid

Weak acid-weak Ethanoic and Aqueous

Strong acid-weak Methyl orange will change sharply at

Weak acid-weak Neither phenolphthalein, not methyl

Vfinal = 50.0 mL + 49.0 mL = 99.0 mL = 0.0990 L

pH = –log(1.0 ´ 10-3) = 3.00

(b) 51.0 mL of 0.100 M NaOH solution have

pOH = –log(1.0 ´ 10-3) = 3.00 )*

3.1 FATTY ACIDS

saturated fatty acids (CnH2n + 1):

omega (ω) fatty acids

3.2 GLYCERIDES - these are glycerol-containing lipids

3.2.1. Neutral glycerides

Triglycerides (or triacylglycerol, TAG)

e.g., Glyceryl tripalmitate (Tripalmitin)

A comparison of saturated and unsaturated fatty acids in some foods

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