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BIOCHEMISTRY OF WATER
Water has many unique properties that make it essential for life. It cover
2/3 of the earth surface. The human body is composed over 70% water and
it is the major component of many body fluids including blood, urine and
saliva.
Structure of water
ﻰ ﻣ
Water has a simple molecular structure. It is composed of two hydrogen
atoms and one oxygen atom attached together by two covalent bonds .The
ا
geometry of water molecules is typically referred to as "bent" or "angular".
ﺳ 2
Since the two bonds connecting oxygen to hydrogen are not linear. The
ﺎ09
bond angle is 104.5◦. Therefore giving a polar trait to water molecules.
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د ﺑﻋ 0
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ظ مﯾ20
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ﻣ
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Chemical and Physical Properties of Water
1-Hydrogen Bonding
Each hydrogen of a water molecule shares an electron pair of the central
oxygen atom. Because oxygen is more electronegative, its nucleus attracts
electrons more strongly than the hydrogen nucleus. The result gives each
hydrogen a partial positive charge, and the oxygen a partial negative
charge. The hydrogen of one water molecule are attracted to the unshared
pairs of electrons of another water molecule. This allows for hydrogen
bonding.
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Concise Medical Biochemistry
ﻰ ﻣ
ﺳ ا 2
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2- Types of non-covalent bonds ﮫ0
ﺑﻋ 0
a- In addition to hydrogen bonds ,other types of non covalent interactions
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ا 1
play important roles to determine the capacity of water to inter act with
macromolecules:
ﻌ ﻟ21
ظ مﯾ20
b- Ionic Interactions: the attraction between acidic (COO-) and basic
(NH3+).
ﻣ 1
c- Hydrophobic Interactions: non-polar molecules cannot form hydrogen
ﺣ07
ﻣ
bonds with water molecules, water tends to squeeze them out.
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d- Van der Waals Interactions : transient unequal distribution of electrons
of any atom leads to transient dipole state .The attraction between this
dipole molecules is greatest at distance called Van der Waals distance
(0.3-0.4nm).
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Concise Medical Biochemistry
3- Universal Solvent
a- Charged Substances
ﻰ ﻣ
ﺳ ا 2
ﺎ09
When a crystal of the ionic compound, NaCl for example, is placed in
ﻣ
water, the sodium and chloride ions are separated in the solvent. The
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hydrogen atoms of water molecules are positively charged and attract
ﻋ
chloride anions. Meanwhile, oxygen atoms of water molecules are
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د
negatively charged and attract sodium cations. Water molecules shield
ا
ﻟ21 1
individual sodium and chloride ions from one another by hydration; thus,
ﻌ
the polarity of water molecules directly affects the dissociation of solutes.
ظ مﯾ20
b- Polar Substances
ﻣ
Due to the dipolar nature of water molecules and its capacity to form
ﺣ07 1
hydrogen bond, the polar molecules can be dissolved very easily. Eg:
ﻣ
Ketones ,Alcohols, Aldehydes, and compounds that have carboxyl or
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amino groups.
c- Amphipathic Substances
Molecules contain polar (head) and non polar groups (tail) eg: soap and
bile salts.
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Concise Medical Biochemistry
ﻰ ﻣ
ﺳ ا 2
ﻣ ﺎ09
molecules cannot dissolve in water except in presence of amphipathic
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molecules eg: fat (TAG) .They can form an emulsion, in which the non
ﻋ
polar molecules are surrounded by the amphipathic molecules which can
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deal with water.
ﻌ ا
ﻟ21
4- Dissociation of water and pH
1
ظ مﯾ20
pH is the negative value of the logarithm of [H+] concentration which is the
number of gram ions of hydrogen per liter.
ﻣ
pH= -log [H+] or [H+] = 10-p
ﺣ07 1
ﻣ
pH range: It starts from 1-14, at pH 7, the number of H+ = OH- and the
ود1
solution is neutral. If the pH is less than 7, so it is acidic, and if the pH is
more than 7, it is alkaline.
Determination of pH:
A- Colorimetric methods:
These methods depend upon the use of indicators which are organic
dyes, which change their color at different pHs. (e.g: phenol red
[yellow in acidic pH and red in alkaline pH]).
1- Indicator paper method:
A piece of filter paper impregnated with an indicator is rapidly
dipped and removed from the unknown solution. The color
obtained is matched with a number if standard colors, each
corresponding to a certain pH (e.g: litmus paper).
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Concise Medical Biochemistry
ﺳ ا
buffer solutions which have different pHs, then matching the
2
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color in the unknown solution with the color of buffer solutions.
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B- ظ مﯾ20
Electrometric method:
ﻣ 1
It depends on the potential difference between positive and negative
ﺣ07
ﻣ
charges, which create an electric potential whose value will reflect
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the pH value of the solution, this by using pH meter.
Buffering against pH changes in biological system
1- Definition:
Buffers are solutions that resist changing their pH in spite of
addition of moderate amount of acid or base.
2-Importance of buffer system:
Enzymes, which control metabolic reactions, are very sensitive
to changes in pH. So, any acid or base formed inside the body
should be rapidly and effectively buffered to allow such
reactions to proceed. This is the function of the physiological
buffer systems present in various tissues and body fluids, the
most important of which being the bicarbonate, phosphate and
protein systems.
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Concise Medical Biochemistry
3-Composition:
Buffers are formed of a weak acid and its salt of strong base, (e.g:
H2CO3 and NaHCO3), or weak base and its salt with strong acid,
(e.g: NH4OH and NH4Cl).
4-Mechanism of action:
A- Addition of strong acid as HCl:
NaHCO3 + HCl H2CO3 + NaCl
B- Addition of strong base as NaOH:
H2CO3 + NaOH NaHCO3 + H2O
ﻰ ﻣ
ا
5-Types of physiological buffers:
ﺳ 2
1- Bicarbonate buffer:
ﻣ ﺎ09
It is carbonic/bicarbonate system (H2CO3/BHCO3) B = base,
(Na+ or K+).
ﮫ0
It is the most important system in the body because:
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a. It is easily produced in high concentration from CO2 of
د
ا 1
metabolic reactions, by carbonic anhydrase enzyme:
ﻌ ﻟ21
H2CO3 carbonic anhydrase CO2 + H2O
ظ مﯾ20
b. At the lungs, due to low CO2 tension, the carbonic
anhydrase reaction is reversed with release of CO2 which is
excreted with expired air.
ﻣ 1
c. Phosphate buffer: BH2PO4/B2HPO4.
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ﻣ
d. Protein buffer: H proteinic acid/ B-proteinate.
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e. Hemoglobin buffer: H Hb/ B Hb.
f. Oxyhemoglobin buffer: H HbO2/B HbO2.
6-Disturbance of buffer system:
The normal blood pH is 7.4, blood buffer systems are so efficient
to keep it constant.
The main buffering system in blood is carbonic/bicarbonate
system which is present in the ratio 1/20.
Bicarbonate is a measure of the alkali available for neutralization
of acids, so it is named as alkali reserve.
Disturbances in buffering systems produce either acidosis or
alkalosis.
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Concise Medical Biochemistry
1) Acidosis:
It is a condition in which there is increase in H2CO3/BHCO3
ratio (more than 1/20).
Types of acidosis:
1- Respiratory acidosis: It is due to:
a. Failure of the lungs to excrete H2CO3 as in bronchial
asthma, massive pneumonia and in asphyxia.
morphia)
ﻰ ﻣ
b. Depression of the respiratory center by toxins, (e.g:
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2- Metabolic acidosis: It is due to:
ﺳ 2
a. Severe muscular exercise with production of large
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amount of lactic acid (lactic acidosis).
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b. High protein diet: This results in the production of
large quantities of sulfuric, phosphor and uric acid.
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c. Ketosis, increased production of ketone bodies
د
ا 1
(acetoacetic acid and hydroxybutyric acid ), occurred
ﻌ ﻟ21
in uncontrolled diabetes mellitus, starvation and
ظ مﯾ20
carbohydrate deficiency.
d. Excessive loss of bases, as in severe diarrhea.
2) Alkalosis:
ﻣ 1
It is a condition in which there is decrease in H2CO3/BHCO3
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ﻣ
ratio (less than 1/20).
ود1
Types of alkalosis:
1- Respiratory alkalosis:
It is usually occurs in all cases of hyperventilation, with
increased loss of CO2 and decreased H2CO3 in blood as in
fevers.
2- Metabolic alkalosis:
It is due to:
a. Loss of acidic gastric juice (contains HCl) by vomiting.
b. Excessive amounts of fruits and vegetables in diet.
c. Administration of Na and K citrates and bicarbonates
for treatment of hyperacidity and peptic ulcer.
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Concise Medical Biochemistry
Acidosis Alkalosisﻣﻰ
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ﻣ ﺎ09
Def: ratio more than 1/20 Def: ﮫratio less0than 1/20
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Causes:
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Causes: 1
1-respiratory acidosis ظﯾ0 1-respiratory alkalosis
م 2
• lung diseases
• depression ﻣof ﺣ
ﻣ
resp center 7
1 Hyperventilation as in fever or hysteria
و
د1 0
2-metabolic acidosis 2-metabolic alkalosis
*Increase of production of acid *Increase of production of bases
Severe muscular exercise excessive fruits and vegetable in diet
High protein diet administration of Na&K citrate or
Ketosis bicarbonate for hyperacidity
*Increase loss of bases as in severe diarrhea *Increase loss of bases as in severe vomiting
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Concise Medical Biochemistry
CHEMISTRY OF CARBOHYDRATES
Carbohydrates present in both plants and animals, they are important
source of energy. Carbohydrates stored in plants in the form of starch,
while in animals in the form of glycogen.
Definition:
ﻣ
Carbohydrates are poly-hydroxy aldehydes or ketones and their derivatives.
ﻰ
Classification:
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ﺎ09
Carbohydrates are classified according to the number of saccharide units as
follows:
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I- Monosaccharides: contain one saccharide unit.
II- Disaccharides: contain two monosaccharide units per molecule.
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III- Oligosaccharides: contain from 3-10 monosaccharide units per
د
molecule.
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IV- Polysaccharides: contain more than 10 monosaccharide units per
ظ مﯾ20
molecule.
ﻣ
I- MONOSACCHARIDES
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ﻣ
Monosaccharides are carbohydrates contain one saccharide unit. They are
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classified according to the number of carbon atoms into trioses, tetroses,
pentoses and hexoses. They are also classified according to the presence of
ketone or aldehyde group into ketoses and aldoses respectively:
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Concise Medical Biochemistry
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CH2OH CH2OH H-C-OH H-C-OH
ﺳ 2 | |
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H-C=O
ظ مﯾ20 CH2OH CH2OH H-C=O
|
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ﺣ07 1 | | |
ﻣ
H-C-OH H-C-OH C=O C=O
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| | | |
H-C-OH HO-C-H H-C-OH HO-C-H
| | | |
H-C-OH H-C-OH H-C-OH H-C-OH
| | | |
CH2OH CH2OH CH2OH CH2OH
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ا
| | | |
ﺳ 2
CH2OH CH2OH CH2OH CH2OH
ﻣ ﺎ09
Glucose Mannose
ﮫ0 Galactose Fructose
ﺑﻋ 0
Monosaccharides of biological importance
د
Monosaccharide
ﻌ ا
ﻟ21 1Biological importance
ظ مﯾ20
Trioses Glyceraldehyde is the mother compound of all aldoses.
Glyceraldehyde-3-phosphate and dihydroxyacetone-
phosphate are formed during glycolysis.
Tetroses
ﻣ
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Erythrose is formed during glucose oxidation.
Pentoses
ﻣ Ribose enters in the structure of RNA.
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Deoxyribose enters in the structure of DNA.
hexoses Glucose: • Enters in the formation of many
disaccharides and polysaccharides.
• It is the main sugar in animal blood.
Galactose: • It forms with glucose the disaccharide
lactose which is present in milk.
• It is found in galactolipids.
Fructose: • It is the sweetest sugar.
• It is present in the seminal fluid.
Mannose: • Enters in the formation of polysaccharides.
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Concise Medical Biochemistry
ﻰ ﻣ
Optical Activity is the ability of a substance, containing one or more
asymmetric carbon atoms, to rotate the plane polarized light (PPL) either to
ا
the left or to the right.
ﺳ 2
Optical activity is measured by polarimeter.
ﻣ ﺎ09
A levorotatory (-) substance rotate the PPL to the left, while the
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dextrorotatory (+) substance rotates the PPL to the right.
Cyclic Forms of Monosaccharides
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Pentoses and hexoses are found to be present in cyclic forms.There are two
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ا 1
cyclic forms, furanose (a four carbon ring) and pyranose (a five carbon
ring).
ﻌ ﻟ21
ظ مﯾ20
Important Derivatives of Monosaccharides
(A) Sugar acids:
1- Aldonic acids: due to oxidation of the aldehyde group (H-C=O →
ﻣ
ﺣ07 1 COOH)
ﻣ
e.g. Glucose → Gluconic acid
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Galactose → Galactonic acid
2- Uronic acids: due to oxidation of the primary alcohol group
(CH2OH→ COOH).
e.g. Glucose → Glucuronic acid
Galactose → Galacturonic acd
3- Aldaric acids: due to oxidation of both aldehyde and primary
alcohol groups.
H-C=O COOH
| |
R → R
| |
CH2OH COOH
e.g. Glucose → Glucaric acid
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Concise Medical Biochemistry
B) Sugar alcohols:
Reduction or addition of hydrogen to monosaccharides produces the
corresponding alcohols.
Glucose → Sorbitol Galactose → Dolcitol
Mannose →Mannitol Ribose → Ribitol
C) Deoxysugars:
One oxygen atom is removed and replaced by hydrogen. The most
removed.
ﻰ ﻣ
common example is deoxyribose in which the oxygen at C2 of ribose is
ا
D) Aminosugars:
ﺳ 2
The OH group at C2 is replaced with amino group (NH2), e.g.
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glucosamine, galactosamine and mannosamine.
E) Ester formation:
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The OH group of monosaccharides can form esters with acids, e.g.
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glucose-1-phosphate and galactose-3-sulfate.
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ﻟ21 1
II- DISACCHARIDES
ظ مﯾ20
Disaccharides consist of two monosaccharide units connected by glycosidic
linkage. They are classified according to their reducing property into:
ﻣ 1
1) Reducing disaccharides: maltose, isomaltose, cellobiose and
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ﻣ
lactose.
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2) Non-reducing disaccharides: sucrose.
A) Maltose: (malt sugar)
It is formed of two glucose units, connected by α1-4 glugosidic bond. It
is hydrolyzed by the action of maltase enzyme into two molecules of
glucose.
Maltose
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Concise Medical Biochemistry
Lactose
ﻰ ﻣ
ﺳ ا
C) Sucrose: (cane sugar or table sugar)
2
ﻣ ﺎ09
It is formed of one fructose and one glucose units, connected by α1-2
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glucosidic bond. Both carbonyl groups (aldehyde group of glucose and
ketone group of fructose) are involved in the linkage, so it is a non-
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reducing sugar. By the action of sucrose (invertase) enzyme, sucrose is
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ا 1
hydrolyzed into glucose and fructose.
ﻌ ﻟ21
ظ مﯾ20 Sucrose
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ﻣ
ود1 III- POLYSACCHARIDES
They contain more than 10 monosaccharide units per molecule. They are
classified into two main groups:
1) Homopolysaccharides: contain only one type of monosaccharide
units.
2) Heteropolysaccharides: contain two or more different
monosaccharide units.
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Concise Medical Biochemistry
HOMOPOLYSACCHARIDES
They are classified according to the name of the building units as follows:
1- Glucans: formed of glucose units, e.g. starch, dextrins, glycogen,
dextrans and cellulose.
2- Fructans: formed of fructose units, e.g. inulin.
A) Starch:
ﻰ ﻣ
It is the storage form of glucose in plants in the form of granules; each
ا
starch granule contains two forms, amylose and amylopectin.
Amylose
ﻣ ﺳ
ﺎ09 2 Amylopectin
granule. ﮫ0
- Present in the inner part of starch - Present in the outer part of starch
granule.
- Forms about 15-20%.
ا 1
- Linear unbranched - Branched polysaccharide.
polysaccharide.
ﻌ ﻟ21
ظ مﯾ20
- Formed of several hundreds of - Formed of several thousands of
glucose units per molecule. glucose units per molecule.
- Glucose units are connected by α - Glucose units are connected by α1-
ﻣ
ﺣ07 1
1-4 glucosidic bonds. 4 glucosidic bonds within the
ﻣ
branches, and α1-6 glucosidic
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bonds at the branching points.
- It gives blue color with iodine. - It gives violet color with iodine.
- More soluble in water. - Less soluble in water.
- Hydrolyzed by amylase to - Hydrolyzed by amylase to maltose
maltose units. and isomaltose units,
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Concise Medical Biochemistry
B) Dextrins:
They are produced during hydrolysis of starch by amylase enzyme.
Starch
Amylase
I2
Maltose + Amylodextrin violet color
Amylase
I2
ﻰ ﻣ
ا
Maltose + Erythrodextrin red color
ﺳ 2
Amylase
ﻣ ﺎ09
I2
ﮫ0
Maltose + Achrodextrin colorless
ﻌ ا
ﻟ21 1
Maltose
C) Glycogen:
ظ مﯾ20
It is the storage form of carbohydrates in animals. It forms 10% of the
ﻣ 1
weight of liver and 2% of skeletal muscles. It is a highly branched
ﺣ07
ﻣ
polysaccharide (more branched than amylopectin); glucose units are
ود1
connected by α1-4 glucosidic bonds within the branches, and α1-6
glucosidic bonds at the branching points. It gives red color with iodine.
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Concise Medical Biochemistry
D) Dextrans:
It is a branched polysaccharide in which glucose unite are connected by
α1-6 glucosidic bonds within the branches and α1-3 or α1-4 glucosidic
bonds at the branching points. Dental plague is rich in dextrans.
Dextrans are also used as components of blood plasma substitutes.
E) Cellulose:
ﻰ ﻣ
It is a linear polysaccharide in which glucose residues are connected by
β 1-4 glucosidic bonds. It cannot be hydrolyzed by human α-amylase
ا
enzyme as it contains β 1-4 glucosidic bonds. Its presence in diet is very
ﺳ 2
important as it increases the bulk of food, thus stimulates intestinal
ﻣ ﺎ09
contractions and prevents constipation.
ﮫ0
HETEROPOLYSACCHARIDES
د ﺑﻋ 0
ا 1
The most important members of this group are the glycosaminoglycans
ﻌ ﻟ21
(GAGS) which contain aminosugars. They are classified into:
ظ مﯾ20
1) Sulfate free GAGS: hyaluronic acid.
2) Sulfate containing GAGS: chondroitin sulfate, dermatan sulfate,
keratan sulfate, heparin and heparn sulfate.
ﻣ
A) Hyaluronic acid:
ﺣ07 1
ﻣ
It is present in the connective tissue, vitreous humour of the eye,
ود1
umbilical cord and synovial fluid. It acts as lubricant and shock
absorbent.
Hyaluronidase enzyme (spread factor) is present in some bacteria and
hydrolyzes hyaluronic acid in the connective tissue allowing the spread
of bacteria. Also, it is present in the caps of sperms to help ovum
fertilization.
B) Chondroitin sulfate:
Present in bone and cartilage.
C) Dermatan sulfate:
Present in skin, blood vessels, heart valves, cornea and sclera.
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Concise Medical Biochemistry
D) Keratan sulfate:
It is present in cartilage and cornea, and it is responsible for corneal
transparency.
E) Heparin:
It is present in high concentrations in mast cells, also present in lung,
liver and arterial wall. It is an anticoagulant.
F) Heparan sulfate:
ﻰ ﻣ
ا
It is present on many cell surfaces commonly bound to protein.
ﻣ ﺳ
ﺎ09 2
ﮫ0
د ﺑﻋ 0
ﻌ ا
ﻟ21 1
ظ مﯾ20
ﻣ
ﺣ07 1
ﻣ
ود1
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Concise Medical Biochemistry
BIOCHEMISTRY OF LIPIDS
Definition: Lipids are biological molecules that are insoluble in aqueous
solutions and soluble in organic solvents.
triacylglycerols.
ﻰ ﻣ
2. They provide energy reserves, predominantly in the form of
ا
3. Both lipids and lipid derivatives serve as vitamins and hormones.
ﺳ 2
4. Bile acids help in lipid solubilization.
ﻣ ﺎ09
ﮫ0
Classification of Lipids
د ﺑﻋ 0
ا 1
1- Simple lipids: esters of fatty acids with alcohols.
ﻌ ﻟ21
2- Compound (conjugated) lipids: esters of fatty acids with alcohols
ظ مﯾ20
and an extra group (phosphate, carbohydrates or proteins).
3- Derived lipids: hydrolytic products of the previous two groups or
substances associated with them in nature.
ﻣ
ﺣ07 1
ﻣ
I-Simple lipids
ود1
These are esters of fatty acids with an alcohol. According to the type of
alcohol, they are classified into:
1- Neutral fats (triacylglycerols TAG or triglycerides TG): esters of
fatty acids with glycerol.
2- Waxes: esters of fatty acids with monohydric alcohol higher than
glycerol.
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Concise Medical Biochemistry
Triacylglycerols
ﻰ ﻣ
ﺳ ا 2
ﻣ ﺎ09
ﮫ0
Pure TAG are colorless, odorless and tasteless. The yellow color and flavor
of TAG is due to association with carotenoids.TAG may be present in the
form of:
د ﺑﻋ 0
ا 1
1- Fats: solid at room temperature due to their high content of saturated
fatty acids.
ﻌ ﻟ21
ظ مﯾ20
2- Oils: Liquid at room temperature due to their high content of
unsaturated fatty acids.
ﻣ
ﺣ07 1 Glycerol
ﻣ
ود1
It is a trihydroxy alcohol. It is colorless, odorless and sweet. It is miscible
with water.
Fatty Acids
Saturated fatty acids of less than eight carbon atoms are liquid at
physiological temperature, whereas those containing more than ten are
ﻰ ﻣ
solid. The presence of double bonds in fatty acids significantly lowers the
melting point relative to a saturated fatty acid.
ﺳ ا 2
ﺎ09
According to presence or absence of double bonds, FA are classified
into:
ﻣ
ﮫ0
I- Saturated fatty acids: Fatty acids that contain no carbon-carbon
ﻋ
double bonds, e.g palmitic (16 C) and stearic (18 C).
ﺑ 0
د
II- Unsaturated fatty acids those that contain double bonds:
ا
ﻟ21 1
a- Mono-ethenoids: contain only one double bond, e.g. oleic acid.
ﻌ
b- Poly-ethenoids are fatty acids with multiple double bonds. They are
ظ مﯾ20
termed polyunsaturated fatty acids (PUFAs).
-Di-ethenoid: e.g. linoleic.
ﻣ
-Tri-ethenoid: e.g. Linolenic.
ﺣ07 1
-Tetra-ethenoid: e.g. Arachidonic
ﻣ
ود1
Nutritional Classification of Fatty Acids:
1- Essential fatty acids; essential in the sense that they must be
provided in the diet. These are linoleic acid and linolenic acid. These
two fatty acids cannot be synthesized from precursors in the body
2- Nonessential Fatty Acids: can be synthesized in the body.
Waxes
Waxes are esters of fatty acids with a monohydroxy alcohol higher than
glycerol, e.g Bee’s wax which is ester of fatty acid with mericyl alcohol (30
C). Lanoline is a wax which covers fur of animals like foxes. It is an ester
of fatty acid with cholesterol.
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Concise Medical Biochemistry
II-Compound Lipids
These are esters of fatty acids with alcohol and an extra group. According
to this extra group, compound lipids are classified into: phospholipids
(containing phosphate), glycolipids (containing carbohydrates) and
proteolipids (containing proteins).
1-Phospholipids
ﻰ ﻣ
ا
The alcohol in phospholipids may be glycerol (glycerophospholipids) or
ﺳ 2
sphingosine (sphingomyelin).
ﻣ ﺎ09
The basic structure of glycerophospolipids is very similar to that of the
ﮫ0
triacylglycerides except that C–3 of the glycerol backbone is esterified to
phosphoric acid. The building block of the phospholipids is phosphatidic
ﺑﻋ 0
acid which results when the X substitution in the basic structure shown in
د
ا 1
the Figure below is a hydrogen atom. Substitutions include ethanolamine
ﻌ ﻟ21
(phosphatidylethanolamine), choline (phosphatidylcholine, also called
ظ مﯾ20
lecithin), serine (phosphatidylserine), glycerol (phosphatidylglycerol), myo-
inositol (phosphatidylinositol), and phosphatidylglycerol (diphosphatidyl-
glycerol more commonly known as cardiolipins).
ﻣ
ﺣ07 1
ﻣ
ود1
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Concise Medical Biochemistry
Phospholipid Structures
ﻰ ﻣ
ﺳ ا 2 Phosphatidylcholine
ﮫ0
د ﺑﻋ 0
ﻌ ا
ﻟ21 1
ظ مﯾ20
Phosphatidylethano-
lamine (PE)
ﻣ
ﺣ07 1
ﻣ
ود1 Phosphatidylserine (PS)
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Concise Medical Biochemistry
Phosphatidylinositol
(PI)
ﻰ ﻣ
ﺳ ا 2
ﻣ ﺎ09 Phosphatidylglycerol
ﮫ0 (PG)
د ﺑﻋ 0
ﻌ ا
ﻟ21 1
ظ مﯾ20 Cardiolipin
(diphosphatidylglycerol,
ﻣ
ﺣ07 1 DPG)
ﻣ
ود1
Lysophospholipids are formed when fatty acid is removed from second
position. Snake venoms contain lecithinase enzyme which converts lecithin
(phosphatidyl choline) to lysolecithin. This leads to hemolysis (break of red
blood corpuscles)
Sphingomyelin is a phospholipid containing sphingosine alcohol (an
amino-alcohol)+ FA + phosphate + choline.
Importance of phospholipids:
1- They are amphipathic molecules. They contain a polar part and a
non-polar part.
2- They help in emulsification of lipids in the intestine, so they help in
digestion and absorption of lipids.
24
Concise Medical Biochemistry
ﻣ
aggregation and the release of serotonin from platelets.
ﻰ
ا
Sphingolipids
ﻣ ﺳ
ﺎ09 2
Sphingolipids are composed of a backbone of sphingosine. Sphingosine is
ﮫ0
esterified to a variety of fatty acids generating a family of molecules
referred to as ceramides. Sphingolipids predominate in the myelin sheath
ﺑﻋ 0
of nerve fibers. The other major class of sphingolipids (besides the
د
ا 1
sphingomyelins) are the glycolipids.
ﻌ ﻟ21
ظ مﯾ20
ﻣ
ﺣ07 1
ﻣ Sphingosine
ود1
Ceramide
25
Concise Medical Biochemistry
2-Glycolipids
ﻰ ﻣ
4-Gangliosides: similar to globosides except they also contain sialic
ا
acid.
ﺳ 2
Importance of glycolpids:
ﻣ ﺎ09
1- They are found in plasma membrane.
ﮫ0
2- They are important component of myelin sheath.
3- Their carbohydrate part plays a role in cell recognition, e.g.
receptors.
د ﺑﻋ 0
ا 1
4- They are an important constituent of nervous system.
ﻌ ﻟ21
ظ مﯾ20
3-Proteolipids
They are formed of a core of lipids surrounded by a lipid layer. So, they are
ﻣ 1
insoluble in water and soluble in fat solvents. They are found mainly in
ﺣ07
ﻣ
nervous tissue.
ود1
N.B.: Lipoproteins are arranged in the opposite way (lipid inside and
protein outside). So they are soluble in water
III-Derived lipids
Sterols.
Vitamins A & D.
3- Squalene: polyunsaturated hydrocarbon containing 30 carbon atoms
produced during the synthesis of cholesterol.
4- Steroids.
5- Carotenoids.
6- Fat soluble vitamins: (A, D, E and K [A and D were mentioned
above as alcohols])
ﻰ ﻣ
ﺳ ا 2
ﻣ ﺎ09
ﮫ0
د ﺑﻋ 0
ﻌ ا
ﻟ21 1
ظ مﯾ20
ﻣ
ﺣ07 1
ﻣ
ود1
27
Concise Medical Biochemistry
STEROIDS
Classification of Steroids
ﻰ ﻣ
ا
Sex Corticoids
Hormones (C21)
ﻣ ﺳ
ﺎ09 2
ﮫ0
Male (C19) Female Glucocorticoi Mineralocorticoi
d ds
د ﺑﻋ 0
ا 1
Estrogen Progesterone
(C18)
ظ مﯾ20
Sterols
Sterols mean solid (ster) alcohols. They are classified to three main groups
according to their presence in nature:
ﻣ 1
Zoo Sterols: present in animals.
ﺣ07
ﻣ
Phytosterols: present in higher plants.
ود1
Mycosterols: present in lower plants e.g. yeast and fungi.
Zoo sterols
28
Concise Medical Biochemistry
Cholesterol:
1- It is formed from activated acetic acid (active acetate). Cholesterol
acts as a precursor of all steroids in animal body.
2- It is widely distributed in all tissues but high concentrations are
present in nervous tissue, liver, adrenals, gonads, skin and adipose
tissue.
3- Normally it is present in plasma in a concentration ranging from 100-
ﻰ ﻣ
200 mg/dL (30% as free cholesterol 70% as cholestryl esters).
Hypercholesterolemia (increase plasma level) predisposes to
ا
atherosclerosis which leads to hypertension.
ﺳ 2
4- It is mainly excreted from the body in bile in the form of bile salts,
ﻣ ﺎ09
less amounts as cholesterol, cholesteryl esters and dihydro-
ﮫ0
cholesterol. In large intestine, cholesterol is reduced by bacteria to
give corpostanol.
ﺑﻋ 0
5- It is converted in the liver to 7-dehydro cholesterol. The latter is
د
ا 1
converted to vitamin D3 under the skin by the action of ultraviolet
rays.
ﻌ ﻟ21
ظ مﯾ20
Phytosterols are present in higher plants and most of them are not
physiologically important.
ﻣ
ﺣ07 1
ﻣ
Mycosterils present in lower plants e.g. yeast and fungi. The most
ود1
important member is ergosterol which is the precursor of vitamin D2.
29
Concise Medical Biochemistry
BILE ACIDS
Types of Bile acids
A- Primary bile acids: These are formed in the liver from cholesterol
and include the following:
1- Cholic acid
2- Chenodeoxycholic acid
B- Secondary Bile Acids: formed by the action of bacteria in large
intestine on primary bile acids, they include:
1- Deoxycholic acid
ﻰ ﻣ
ا
2- Lithocholic acid
ﺳ 2
Bile Salts:
ﻣ ﺎ09
Bile salts are formed by the conjugation of bile acids with glycine (80%) or
ﮫ0
taurine (20%). Then they are excreted by liver in bile as sodium salts e.g.
sodium glycocholate and sodium taurocholate. Bile salts pass to the
ﺑﻋ 0
intestine where they are reabsorbed and return back to the liver to be
د
ا 1
excreted again in bile (enterohepatic circulation of bile).
ﻌ ﻟ21
ظ مﯾ20
ﻣ
ﺣ07 1
ﻣ
ود1
Importance of bile salts:
1- Conversion to bile salts is an important mechanism for removal of
cholesterol from the body.
2- Emulsification of fat in the intestine which is essential for their
digestion and absorption.
3- Prevent precipitation of cholesterol in bile and formation of
cholesterol stone.
4- They stimulate the liver to secrete more bile. (choleretic effect).
30
Concise Medical Biochemistry
STEROID HORMONES
1- Sex Hormones
ﻰ ﻣ
ﺳ ا 2
ﻣ ﺎ09
Testosterone
ﮫ0
The main hormone secreted by the testes is testosterone. It acts as a
ﺑﻋ 0
prohormone. It is converted in target cells by reduction of ring A to
د
ا
ﻟ21 1
dihydrotestosterone (DHT) which is the active form.
ﻌ
Other androgens which are formed in the body include:
ظ مﯾ20
Androstenedione
Androsterone, Epindrosterone and Dehydroepiandrosterone
(DHEA)
ﻣ
ﺣ07 1
Some androgens are formed in the ovaries and the adrenal cortex.
ﻣ
B) Female sex hormones:
ود1
Estradiol Progesterone
31
Concise Medical Biochemistry
Estrogens (18 C)
The most potent is estradiol, which is the main hormone secreted by the
ovaries. It is also formed by the placenta during pregnancy. Small
amounts are formed in the testis and the adrenal cortex.
It is converted to the less active products, estrone and estriol in the liver
which are excreted in urine in conjugation with glucuronic acid or
sulfate.
Progesterone (21 C)
ﻰ ﻣ
It is secreted in females mainly by the ovaries after ovulation and
ا
formation of corpus luteum and by placenta during pregnancy. It is
ﺳ 2
converted in the liver to pregnanediol (inactive product) which is
excreted in urine.
ﻣ ﺎ09
ﮫ0
2- Adrenal Cortical Hormones (Corticoids)
د ﺑﻋ 0
ا 1
Corticoids are mainly formed and secreted by the adrenal (suprarenal)
ﻌ ﻟ21
cortex. They are classified according to their action into two types
ظ مﯾ20
(Glucocorticoids and mineralocorticoids).
A) Glucocorticoids (21 C): They are termed glucocorticoids because
they increase blood glucose level. They are derivatives of
ﻣ 1
Corticosterone and include:
ﺣ07
ﻣ
1- Corticosterone
ود1
2- Cortisol the most potent one
3- Cortisone
Cortisol
32
Concise Medical Biochemistry
ﻰ ﻣ
ﺳ ا 2
ﻣ ﺎ09
ﮫ0
د ﺑﻋ 0
ﻌ ا
ﻟ21 1
ظ مﯾ20
ﻣ
ﺣ07 1
ﻣ
ود1
33
Concise Medical Biochemistry
AMINO ACIDS
Amino acids are the building blocks of proteins. All proteins are composed
of 20 different amino acid types commonly obtained upon hydrolysis of
proteins (>100 types have been isolated) and referred to as α-amino acids.
Their general structure is shown below:
R
|
ﻰ ﻣ
ا
H2N—C —COOH
ﺳ 2 |
ﻣ ﺎ09 H
ﮫ0
L - α - amino acid
ﺑﻋ 0
Amino acids are classified into different ways based on polarity, structure,
د
ا 1
nutritional requirement, metabolic fate, etc. Generally used classification is
based on polarity.
ﻌ ﻟ21
ظ مﯾ20
I-Based on polarity, amino acids are classified into four groups:
1-Non-polar amino acids
ﻣ 1
They have equal number of amino and carboxyl groups and are neutral.
ﺣ07
ﻣ
These amino acids are hydrophobic and have no charge on the 'R' group.
ود1
The amino acids in this group are alanine, valine, leucine, isoleucine,
phenyl alanine, glycine, tryptophan, methionine and proline.
34
Concise Medical Biochemistry
ﻰ ﻣ
ﺳ ا 2
ﻣ ﺎ09
2- Polar amino acids with no charge
ﮫ0
These amino acids do not have any charge on the 'R' group. These amino
acids participate in hydrogen bonding of protein structure. The amino acids
ﺑﻋ 0
in this group are - serine, threonine, tyrosine, cysteine, glutamine and
د
aspargine.
ﻌ ا
ﻟ21 1
ظ مﯾ20
ﻣ
ﺣ07 1
ﻣ
ود1
3- Polar amino acids with positive charge
Polar amino acids with positive charge have more amino groups as
compared to carboxyl groups making them basic.
The amino acids, which have positive charge on the 'R' group are placed in
this category. They are lysine, arginine and histidine.
35
Concise Medical Biochemistry
ﻰ ﻣ
ا
4- Polar amino acids with negative charge
ﺳ 2
Polar amino acids with negative charge have more carboxyl groups than
amino groups making them acidic.
ﻣ ﺎ09
ﮫ0
The amino acids, which have negative charge on the 'R' group are placed in
this category. They are called as dicarboxylic mono-amino acids. They are
ﺑﻋ
aspartic acid and glutamic acid.
د
0
N.B:
ﻌ ا
ﻟ21 1
ظ مﯾ20
1-Branched chain amino acids: Valine, leucine and isoleucine.
2- OH containing amino acids: serine, threonine and tyrosine.
3-Sulfur containing amino acids: Cysteine and methionine.
ﻣ
ﺣ07 1
4- Aromatic amino acids: Phenylalanine, tyrosine and tryptophan.
ﻣ
5- Heterocyclic amino acids: Histidine and tryptophan.
ود1
6- Heterocyclic imino aicd: Proline.
BIOCHEMISTRY OF PROTEINS
Definition: Proteins are polymers of amino acids covalently linked through
peptide bonds into a chain.
Functions of proteins:
1-Antibodies - are specialized proteins involved in defending the body
from antigens (foreign invaders).
ﻰ ﻣ
2-Contractile Proteins - are responsible for movement. Examples include
ا
actin and myosin. These proteins are involved in muscle contraction and
ﺳ 2
movement.
ﻣ ﺎ09
3-Enzymes - are proteins that facilitate biochemical reactions. They are
ﮫ0
often referred to as catalysts because they speed up chemical reactions.
4-Hormonal Proteins - are messenger proteins which help to coordinate
ﺑﻋ 0
certain bodily activities. Examples include insulin, oxytocin, and
د
ا 1
somatotropin. Insulin regulates glucose metabolism by controlling the
ﻌ ﻟ21
blood-sugar concentration. Oxytocin stimulates contractions in females
ظ مﯾ20
during childbirth. Somatotropin is a growth hormone that stimulates protein
production in muscle cells.
5-Structural Proteins - are fibrous and stringy and provide support.
ﻣ 1
Examples include keratin, collagen, and elastin. Keratins strengthen
ﺣ07
ﻣ
protective coverings such as hair, quills, feathers, horns, and beaks.
ود1
Collagens and elastin provide support for connective tissues such as
tendons and ligaments.
6-Storage Proteins - store amino acids. Examples include ovalbumin and
casein. Ovalbumin is found in egg whites and casein is a milk-based
protein.
7-Transport Proteins - are carrier proteins which move molecules from
one place to another around the body. Examples include hemoglobin and
cytochromes. Hemoglobin transports oxygen through the blood.
Cytochromes operate in the electron transport chain as electron carrier
proteins.
37
Concise Medical Biochemistry
ﻰ ﻣ
ﺳ ا 2
ﻣ ﺎ09
ﮫ0
ﺑﻋ 0
The head-to-tail arrangement of amino acids in a protein means that there is
د
ا
ﻟ21 1
an amino group on one end (called the amino-terminus or N-terminus) and
ﻌ
a carboxyl group on the other end (carboxyl-terminus or C-terminus).
ظ مﯾ20
Levels of Protein Structure:
ﻣ
Primary structure: the linear arrangement of amino acids in a
ﺣ07 1
protein. The bond stabilizing this level is peptide bond.
ﻣ
Secondary structure: areas of folding or coiling within a protein;
ود1
examples include alpha helices and pleated sheets, which are
stabilized by hydrogen bonding.
Tertiary structure: folding of the protein to give the final three-
dimensional structure of a protein. It results from a large number of
interactions between amino acids e.g. hydrophobic interactions,
electrostatic. Hydrogen bonds and di-sulfide bond.
38
Concise Medical Biochemistry
Denaturation of Proteins:
Definition: It is destruction of secondary, tertiary and-if present-
quaternary structure of proteins.
Denaturating agents:
1-Physical: e.g. heat, U.V. rays and repeated freezing and thawing.
2-Chemical: e.g. conc. Acids and alkalis, strong salt solutions and salts of
heavy metals.
Effects of denaturation:
ﻰ ﻣ
The protein becomes less soluble, more viscous and more digestible. If the
ا
protein has a biological function, e.g. enzyme or hormone, it will lose its
ﺳ 2
function.
ﻣ ﺎ09
ﮫ0
Classification of Proteins
1-Simple proteins.
د ﺑﻋ 0
ا 1
2-Conjugated proteins.
3-Derived proteins.
ﻌ ﻟ21
ظ مﯾ20 Simple Proteins
ﻣ 1
On hydrolysis, they produce amino acids only.
ﺣ07
ﻣ
1-Albumins and globulins:
ود1
These are coagulable proteins. They are of high biological value (contain
all essential amino acids). Albumins are precipitated by full saturation with
ammonium sulfate, but globulins are precipitated by half
saturation.Examples: Plasma albumin and globulins and lactalbumin and
lactglobulin in milk.
2-Scleroproteins:
These are insoluble fibrous proteins having protective or supportive
function. They include keratin (in skin), collagen (in tendons, ligaments
and bones) and elastin (in walls of blood vessels and in lung).
39
Concise Medical Biochemistry
Conjugated Proteins
1- Phosphoproteins:
ﻰ ﻣ
ا
• They have a phosphate prosthetic group e.g. casein of milk,
ﺳ 2
phosphorylation of enzyme is a way of regulating their activity.
2- Lipoproteins:
ﻣ ﺎ09
ﮫ0
• They are formed of lipids and proteins where proteins are present in
the outer layer making them water soluble e.g. Plasma proteins
3- Glycoproteins:
د ﺑﻋ 0
ا 1
• They are proteins containing carbohydrate group, e.g. blood group
ﻌ ﻟ21
substance and immunoglobulins.
ظ مﯾ20
4- Metalloproteins:
• These are proteins containing a metal prosthetic group. According to
the type of metal present (Fe, Cu, Mg, Mn and Zn) they are further
ﻣ
divided into :
ﺣ07 1
ﻣ
i. Metalloproteins containing iron:
ود1
1. Non heme iron containing proteins (NHI):
a. They include:
i. Ferritin (storage form of iron)
ii. Transferrin (transport form of iron)
iii. Hemosiderin (in cases of iron toxicity)
2. Hemoproteins:
a. These are proteins containing iron in the form of heme.
They include haemoglobin (in blood), Myoglobin (in
muscles) and some enzymes, e.g. Cytochromes, catalase,
peroxidase and tryptophan pyrollase.
b. Haemoglobin: it is found in red blood cells. It carries
oxygen from lungs to tissues and carbon dioxide from
tissues to lungs, it also acts as a buffer system that helps to
40
Concise Medical Biochemistry
ﻰ
insulin in pancreas, carbonic anhydrase and alcoholﻣ
iii. Metalloproteins containing Zinc (Zn): Include the storage form of
ا
dehydrogenase
ﺳ 2
iv. Metalloproteins containing Manganese (Mn): such as arginase,
ﻣ ﺎ09
carboxylase and decarboxylase.
ﮫ0
v. Metalloproteins containing Magnesium (Mg): as kinases,
phosphatases and phosphorylases.
ﺑﻋ 0
5- Chromoproteins: these are colored proteins:
د
ا 1
• Metallochromoproteins: those containing iron are red and
ﻌ ﻟ21
chlorophylls in plants are green.
ظ مﯾ20
• Nonmetallochromoproteins:
i. Flavoproteins (containing FMN or FAD prosthetic group) are
yellow. E.g. D-amino acid oxidase and L-amino acid oxidase.
ﻣ 1
ii. Carotenoids such as the visual pigment present in retina.
ﺣ07
ﻣ
6- Nucleoproteins: these are proteins bound to DNA or RNA. They are
ود1
basic proteins being rich in arginine, lysine and hitidine.
Derived Proteins
41
Concise Medical Biochemistry
A- Collagen :
ﻰ ﻣ
ﺳ ا
It is present in skin, bones, lungs, tendons, vessels and cornea. It is formed
2
ﻣ ﺎ09
by connective tissue, there are more than 15 type of collagen and represent
25 % of total body proteins.
ﮫ0
ﺑﻋ 0
The basic structural unit of collagen is tropocollagen , which is made of 3
د
ا
ﻟ21 1
polypeptide chains named alpha chain.
ﻌ
ظ مﯾ20
ﻣ
ﺣ07 1
ﻣ
ود1
42
Concise Medical Biochemistry
Tropocollagen:
It is a triple helix molecule contains 3 alpha chains; about 300 nm in
length and 1.5 nm in diameter, each chain is twisted in the form of a
tight left-handed - helix with only 3 amino acids in each turn.
Typical amino acid sequence is Glycine , Proline&Hydroxyproline.
ﻰ ﻣ
Collagen is a protein of low biological value, and it is non-digestible.
ﺳ ا
Boiling converts it to gelatin which is soluble in H2O and digestible.
2
ﻣ ﺎ09
ﮫ0
د ﺑﻋ 0
ﻌ ا
ﻟ21 1
ظ مﯾ20
ﻣ
ﺣ07 1
ﻣ
ود1
43
Concise Medical Biochemistry
B- Elastin:
It is a rubber like protein. It is present in elastic connective tissue of
ligaments, lungs and walls of blood vessels.
It is formed of 4 polypeptide chains interconnected through their
lysine residues, 4 of them are linked together to form cyclic structure
termed Desmosine.
ﻰ ﻣ
C- Fibronectin
ﺳ ا 2
ﺎ09
It is glycoprotien of extra cellular matrix.
ﻣ
ﮫ0
It consists of 2 identical subunits joined by 2 disulfide bridges.
ﻋ
It binds to collagen, cell receptor and heparin.
ﺑ 0
ا د
ﻟ21 1 Bone protein
ﻌ
ظ مﯾ20
A- collagen protiens:
1- collagen type 1(main bone protein)
ﻣ
2- collagen type V
ﺣ07 1
ﻣ
B-other protiens :
ود1
1- plasma protiens
2- proteoglycans
3- osteonectin
Cartilage proteins
A- collagen proteins:
1- collagen type 11(main cartilage protein)
2- collagen type V,VI,IX
B-other proteins :
1- aggrecans ,it is GAGs attached to protein
2- chondronectin
44