SYSTEMS PLUS COLLEGE FOUNDATION

Angeles City
COLLEGE OF NURSING

MC2: BIOCHEMISTRY
1st Semester, S.Y. 2021-2022

HANDOUT No.2: THE PROTEIN AND AMINO ACIDS

I. LEARNING OUTCOMES

At the end of this lecture, the students should be able to:

1. Explain the importance of protein and amino acid.

2. Identify the types and classifications of protein.
3. Identify the different amino acids.

II. CONTENT

PROTEIN
Proteins are present in every cell of humans, animals, plant tissues, tissue fluids and in micro-
organisms. They account for about 50% of the dry weight of a cell. The term protein is derived from the
Greek word proteios meaning holding first place or rank in living matter.

MEDICAL AND BIOLOGICAL IMPORTANCE

>Proteins perform wide range of essential functions in mammalians.
1. Proteins are involved in the transport of substances in the body.
2. Enzymes which catalyze chemical reactions in the body are proteins.
3. Proteins are involved in defense function. They act against bacterial or viral infection.
2. Hormones are proteins. They control many biochemical events.
3. Some proteins have role in contraction of muscles.
4. Proteins are involved in the gene expression. They control gene expression and
translation.
5. Proteins serve as nutrients. Proteins are also involved in storage function.
6. Proteins act as buffers.
7. Proteins function as anti-vitamins.
8. Proteins are infective agents.
9. Some toxins are proteins.
10. Some proteins provide structural strength and elasticity to the organs and vascular system.

11. Some proteins are components of structures of tissues.

CLASSIFICATION OF PROTEINS
There is no single universally satisfactory system of protein classification so far.
1. One system classifies proteins according to their composition or structure.
2. One system classifies them according to solubility.
3. One system classifies them according to their shape.
4. Classification of proteins based on their function also found in literature.

Classification of proteins based on their composition

Proteins are divided into three major classes according to their structure.
1. Simple proteins: Simple proteins are made up of amino acids only. On hydrolysis, they yield
only amino acids.
a. Examples: Human plasma albumin, Trypsin, Chymotrypsin, pepsin, insulin,
soyabean
b. trypsin inhibitor and ribonuclease.

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 2. Conjugated proteins: They are proteins containing non-protein part attached to the protein part.
The non-protein part is linked to protein through covalent bond, non-covalent bond and
hydrophobic interaction. The non-protein part is loosely called as prosthetic group. On
hydrolysis, these proteins yield non-protein compounds and amino acids.
Conjugated Protein-> Protein + Prosthetic Group

3. Derived proteins: As the name implies this class of proteins are formed from simple and
conjugated proteins. There are two classes of derived proteins.
(i) Primary derived proteins: They are formed from natural proteins by the action of
heat or alcohol etc. The peptide bonds are not hydrolysed. They are synonymous
with denatured proteins.
a. Example: Coagulated proteins like cooked-egg albumin.
(ii) Secondary derived proteins: They are formed from partial hydrolysis of proteins.
b. Examples: Proteoses, peptone, gelatin, and peptides.

Proteins classification according to their solubility

1. Albumins
2. Globulins
3. Glutelins
4. Protamins
5. Histones
6. Prolamines
7. Sclero proteins

Classification of proteins based on shape

Proteins are divided into two classes based on their shape.

1. Globular proteins: Polypeptide chain(s) of these proteins are folded into compact globular
(Spherical) shape.
2. Fibrous proteins: Poly peptide chains are extended along one axis.

PLASMA PROTEIN
Plasma is non-cellular portion of blood. The total plasma protein level ranges from 6-7 gm/dl.
Plasma contains many structurally and functionally different proteins. Plasma proteins are divided into two
categories.
1. Albumin
2. Globulin

Characteristics of Plasma Proteins

1. They are all glycoproteins except albumin. Sialic acid is the most important of all the sugars
present in plasma proteins. Removal of sialic acid decreases the life span of plasma proteins.
2. Each plasma protein has defined life span. The half-life of albumin is 20 days and haptoglobin life
span is 15 days.
3. Liver is the sole source of albumin, prothrombin and fibrinogen. Most of the a and b globulins are
also of hepatic origin. Y-globulins are derived from lymphocytes.

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Albumin
Liver produces about 12 gms of albumin per day.

Functions
1. Albumin accounts for 75% of the osmotic pressure (25 mm Hg) in blood and responsible for
maintenance of blood volume.
2. Albumin has major role in the regulation of fluid distribution.
3. One gram of albumin holds 18 ml of fluid in the blood stream. Decrease in albumin level leads to
accumulation of fluid which results in edema.
4. It transports fatty acids from adipose tissue to liver. Albumin also binds many hydrophobic
substances like bilirubin and several drugs. The binding of bilirubin is critical in neo-natal period.
5. Albumin acts as a reservoir for Ca2+ in plasma. About 40% of plasma calcium is bound to albumin.
6. Albumin is also involved in the transport of thyroid hormones, glucocorticoids and sex
steroids.
7. Albumin functions as protein source for peripheral tissues. Each day liver replaces about 12 gm of
albumin taken up by peripheral tissues. In certain conditions like stress and starvation the turnover
rate of albumin is increased. Albumin is in dynamic equilibrium.
8. Albumin acts as a buffer.
a1-Globulin
 Mainly a1-antitrypsin. It is a protease inhibitor.
 It is the major component of a1-fraction and accounts more than 90%.
 It inhibits trypsin, chymotrypsin, elastase and neutral protease.
 The major function of a1-antitrypsin is the protection of pulmonary tissue and other tissues from the
destructive action of proteases.
 Deficiency of a1-antitrypsin results in emphysema.

a1-Acid glycoprotein (AAG): It is another major component of α1-globulins. It increases in plasma in

inflammatory conditions.

Other components of a1-globulins are:

 a-Lipoprotein
 Prothrombin
 Retinolbinding protein
 Thyroxine binding globulin
 a1-Fetoprotein
 a2-Globulins
 Haptoglobulin
 Kidney cannot filter haemoglobin-haptoglobin complex because of its larger size.
 a2-Macroglobulin
 Ceruloplasmin
 Erythropoietin
 Pseudocholinesterase
b-Globulins: They are
 Transferrin
 b-Lipoproteins
 Complement-3

Other globulins present in plasma are:

 Fibrinogen
 Prealbumin

IMMUNOGLOBULINS

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 They are globulins produced as body’s immune or defense against infection. Invasion of body by
virus or microorganisms or foreign molecules is called infection. They are produced by B-lymphocytes,
bone marrow and spleen in response to infection. Entry of foreign molecule into body triggers the synthesis
of specific globulin, which selectively combines with foreign molecule and lead to its inactivation. The
foreign molecule is called as antigen whereas globulin produced against it is called as antibody. Even
without infection the normal plasma contains hundreds of different antibody molecules.

AMINO ACIDS

OCCURRENCE
Amino acids and peptides are present in humans, animals, tissues, blood, microorganisms and plants.

MEDICAL AND BIOLOGICAL IMPORTANCE

1. Amino acids serve as building blocks of proteins. Some amino acids are found in free form in
human blood.
2. They also serve as precursors of hormones, purines, pyrimidines, porphyrins, vitamins and
biologically important amines like histamine.
3. Peptides have many important biological functions. Some of them are hormones. They are
used as anti-biotics and antitumor agents.
4. Some peptides are required for detoxification reactions. Some peptides serve as
neurotransmitters.
5. Amino acid proline protects living organisms against free radical induced damage.
6. Some peptides are involved in regulation of cell cycle and apoptosis.
7. Peptides of vertebrates and invertebrates act as antimicrobial agents. They are part of innate
immunity. Bacterial infections at epithelial surface induce production of antimicrobial peptides,
which cause lysis of microbes.
8. Peptides are enzyme inhibitors. Natural and synthetic peptide inhibitors of angiotensin
converting enzyme (ACE) act as a anti hypertensives. Peptide inhibitors of ACE present in
physiological foods, lowers blood pressure after they are absorbed from intestine. Lisinopril,
Enalapril etc. are synthetic peptide inhibitors of ACE that are used as drugs in the treatment of
hypertension.
9. Some synthetic peptides are used as enzyme substrates
KINDS OF AMINO ACID

Valine, Leucine & Isoleucine

 All of these 3 amino acids are called branched chain amino acids (BCAAs).
 They perform the important functions of increasing proteins and serving as an energy source
during exercise.

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  BCAAs are amino acids present largely in myoproteins.

Alanine
 An important amino acid as it is an energy source for the liver.
 One of the amino acids which most easily used as an energy source.
 Reported to improve alcohol metabolism.
 Used as a material for synthesis of glucose (blood sugar) needed by the body.
 Essential to the health of the liver.

Arginine
 An amino acid needed to maintain normal functions of blood vessels and other organs.
 Plays an important role in expanding blood vessels to facilitate the blood flow.
 Nitric oxide, which is required to expand blood vessels, is made from arginine.
 An amino acid that is useful in eliminating excessive ammonia from the body.
 Reported to enhance immunological function.
 Arginine possesses various functions, which the body utilizes when necessary; like when blood
flow is insufficient during exercise; or when ammonia, a fatigue-causing substance, is increased; or
when body resistance is likely to decrease.

Glutamine
 An amino acid needed to maintain normal functions of the gastrointestinal tract and muscles.
 One of the amino acids contained most abundantly in the body.
 Plays a role in protecting the stomach and intestinal tract.
 Used as an energy source for the intestinal tract in particular.
 Reported to protect the liver and to increase alcohol metabolism.
 Essential to the health of the liver
 Glutamine is used as an energy source for the intestine and is an indispensable component to
maintain its normal function. This amino acid is also used to enhance liver function.

Lysine
 It is a representative essential amino acid.
 Tends to be insufficient when we are on a diet centered on bread or rice.
 Deficient in flour and polished rice.
 Flour lacks lysine the most, especially when compared to the ideal amino acid pattern.
 The deficient amino acid should be supplemented to enhance nutritional value.
 A project by the United Nations University has shown that lysine tends to be deficient in developing
countries where people depend on flour as their protein source.
 If amino acids such as lysine are deficient it may lead to growth failure.

Aspartic acid
 Contained in asparagus in large amounts.
 An amino acid which is most easily used as an energy source.
 Maybe used as an ingredient of nutrient preparations.
 Aspartic acid is an amino acid which is located most closely to the TCA cycle, the site of energy
production.
 The TCA cycle can be likened to the engine of a car. Based on this mechanism, each of our body
cells generates energy.

Glutamic Acid
 Glutamic acid is often referred to as Glutamate.
 Contained in wheat and soybean in large amounts.
 An amino acid which is most easily used as an energy source.
 An important taste component of Japanese stock soup. It is contained in various natural foods.
 Reported to accelerate early recovery from fatigue during exercise.

Proline
 The main component of “collagen” which constitutes the skin and other tissues.
 Serves as a fast-acting energy source.

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  Proline is a most important amino acid as a natural moisturizing factor that brings moisture to the
skin

Cysteine
 Cysteine is easy to be deficient in the infants.
 Synthesized from methionine in the human body.
 With infants the ability of this cysteine synthesis activity is not sufficient.

Threonine
 An essential amino acid which is used to form active sites of enzymes.

Methionine
 An essential amino acid which is used to produce various substances needed by the body.

Histidine
 An essential amino acid which is used to produce histamine and others.

Phenylalanine
 An essential amino acid which is used to produce various useful amines.

Tyrosine
 Used to produce various useful amines and is sometimes called aromatic amino acid together with
phenylalanine and tryptophan.

Tryptophan
 An essential amino acid which is used to produce various useful amines.

Asparagine
 It is an amino acid which is located close to the TCA cycle (place of energy generation) together
with aspartic acid.

Glycine
 Used to produce glutathione and porphyrin, a component of hemoglobin.

PEPTIDE
1. Peptides consist of 2 or more amino acid residues linked by peptide bond.
2. A peptide bond is formed when carboxyl group of an amino acid react with a-amino group of
another amino acid. (Fig. 2.12). Peptide bond formation between two amino acids is always
accompanied by loss of one water molecule. Further, peptide and proteins contain an amino (N–)
terminus and carboxy (C–) terminus.
3. A peptide or protein is named starting with N-terminal amino acid and usually the N-terminal is
located on the left-hand side.
4. Animal, plant and bacterial cells contain wide variety of low molecular weight peptides (2-10 amino
acids residues) having profound biological functions.

TOXIC PEPTIDES
1. Some peptides act as toxins.
2. a-amanitin is a bicyclic octapeptide present in a particular variety of mushrooms. It is
extremely toxic to humans.
3. It is responsible for mushroom poisoning cases around the world.

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 4. When the mushrooms are consumed it causes pain in the gastrointestinal tract, vomiting,
diarrhea and nausea.
5. Death occurs within a week due of impairment of liver and kidney functions.

CYCLOTIDES (CYCLIC PEPTIDES)

In some peptide’s disulfide bonds are more. These disulfide bonds create knot with in the
molecule. Two disulfide bonds and their connecting back bone segment form ring. They are known as
cyclotides. These cyclic peptides show diverse actions. Some are anti-HIV, anti-bacterial and insecticidal
agents. Some examples are given below:
1. Sunflower trypsin inhibitor (SFTI)
2. RTD-1
3. Microsin

III. KEY POINTS FOR REVIEW

 Protein and Amino Acids have different functions.
 There are different classifications of protein in the body.
 There are 19 identified prominent amino acid of the body.

IV. TEST YOUR KNOWLEDGE

1) The liver produces how many grams of albumin?

a) 9 gms
b) 10 gms
c) 11 gms
d) 12 gms

2) Invasion of body by virus or microorganisms or foreign molecules is called:

a) Infestation
b) Infection
c) Intervention
d) Ingestion

3) This immunoglobulin protects the client from intestinal parasitism.

a) IgM
b) IgE
c) IgG
d) IgD

V. READINGS AND REFERENCES

Smith, M. Biochemistry: An Organic Chemistry Approach. CRC Press Taylor and Francis Group

Takemura, M. (2011). The Manga Guide for Biochemistry. Ohmsha Ltd. Tokyo, Japan

Vasudevan, DM, Sreekumari, S., & Vaidyanattan, K. (2013). Textbook of Biochemistry for Medical
Students. Jaypee Brothers Medical Publishers (P) Ltd.

ONLINE RESOURCE:

https://courses.lumenlearning.com/boundless-biology/chapter/antibodies/

Prepared by:

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MARY JANE T. CABATAÑA, RN
Instructor, MC2
1ST Semester, S.Y. 2021-2022

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