CLASSIFICATION OF

PROTEIN Part- 7
SOURCES OF PROTEIN
• Exogenous proteins, following ingestion, serve as sources of the essential amino acids
and are the primary source of the additional nitrogen needed to synthesise the
nonessential amino acids and nitrogen-containing compounds.
• Dietary or exogenous sources of protein include:
• Animal products such as meat, poultry, fish, and dairy products (with the
exception of butter, sour cream, and cream cheese)
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Plant products such as grains, grain products, legumes, and vegetables
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• Endogenous proteins presented to the digestive tract represent another source of
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amino acids and nitrogen, and they mix with exogenous nitrogen sources.
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• Endogenous proteins include:

• desquamated mucosal cells, which generate about 50 g of protein per day
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• digestive enzymes and glycoproteins, which generate about 17 g of protein

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each day
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• The digestive enzymes and glycoproteins are derived from digestive secretions of the
salivary glands, stomach, intestine, biliary tract, and pancreas.
• Most of these endogenous proteins, which may total about 70 g or more per day, are
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digested and provide amino acids available for absorption.

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• Digestion of protein and absorption of amino acids are crucial for optimal protein
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nutriture.
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DAILY REQUIREMENT OF PROTEIN

• Protein and amino acid requirements of humans are influenced by age, body size, and
physiological state, as well as by the level of energy intake.
• The recommended dietary allowance for protein for adults is 0.8 g protein per kg
body weight per day.
 FUNCTIONS OF PROTEIN

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CATALYSTS
• Enzymes are protein molecules that act as catalysts: they change the rate of reactions
occurring in the body.
• Enzymes are found both intracellularly and extracellularly, such as in the blood.
• Enzymes are frequently classified according to the type of reactions that they catalyse.
 • For example: Hydrolases cleave compounds, Isomerases transfer atoms within a
molecule, Ligases (synthases) join compounds, Oxidoreductases transfer electrons,
Transferases move functional groups.
• They are constructed so that they combine selectively with other molecules (called
substrates) in the cell.
• The active site on the enzyme (a small region usually in a crevice of the enzyme) is
where the enzyme and substrate bind and the product is generated.
• Some enzymes, however, require a cofactor or coenzyme to carry out the reaction.
• Minerals such as zinc, iron, and copper function as cofactors for some enzymes.

MESSENGERS
• Some proteins are hormones.

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• Hormones act as chemical messengers. Pl
• They are synthesised and secreted by endocrine tissue (glands) and transported in the
blood to target tissues or organs, where they bind to protein receptors.
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• Hormones generally regulate metabolic processes.

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• Whereas some hormones are derived from cholesterol and classified as steroid
hormones, others are derived from one or more amino acids.
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• The amino acid tyrosine, for example, is used along with the mineral iodine to
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synthesise the thyroid hormones.

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• Tyrosine is also used to synthesise the catecholamines, including dopamine,

norepinephrine, and epinephrine.
• The hormone melatonin is derived in the brain from the amino acid tryptophan.
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• Other hormones are made up of one or more polypeptide chains.

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• Insulin, for example, consists of two polypeptide chains linked by a disulfide bridge.
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• Glucagon, parathyroid hormone, and calcitonin each consist of a single polypeptide

chain.
• Many other peptide hormones, such as adrenocorticotropic hormone(ACTH),
somatotropin (growth hormone), and vasopressin (also known as antidiuretic
hormone, ADH), have important roles in human metabolism and nutrition.

STRUCTURAL ELEMENTS
 • Several proteins have structural roles in the body. Some of these proteins include:
contractile proteins, fibrous proteins, globular proteins
• The two main contractile proteins, actin and myosin, are found in cardiac, skeletal,
and smooth muscles.
• Fibrous proteins, which tend to be somewhat linear in shape, include collagen, elastin,
and keratin and are found in bone, teeth, skin, tendons, cartilage, blood vessels, hair,
and nails.
• Each type of collagen is made of three polypeptide (tropocollagen) chains that are
cross-linked for strength.
• The amino acid composition of the chains is rich in the amino acids glycine and
proline.
• In addition, collagen contains two hydroxylated amino acids—hydroxylysine and
hydroxyproline—that are not found in other proteins.
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Collagen polypeptides are also attached to carbohydrate chains and thus are
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considered to be glycoproteins.
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• Other structural proteins, such as elastin, are associated with proteoglycans.

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• Globular proteins are named for their spherical shape.

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• Although they vary to some degree, depending on the exact protein, globular proteins
generally contain multiple α- helices and β-pleated sheets
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• Some examples of globular proteins include myoglobin, calmodulin, and many

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enzymes.

IMMUNOPROTECTORS
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• Immunoprotection is provided to the body in part by a group of proteins called

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immunoproteins, also called immunoglobulins (Ig) or antibodies (Ab).

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• These immunoproteins, of which there are five major classes (IgG, IgA, IgM, IgE,
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and IgD), are Y-shaped proteins made of four polypeptide chains (two small chains
called light [L] chains and two large chains called heavy [H] chains).
• The immunoglobulins are produced by plasma cells derived from B-lymphocytes, a
type of white blood cell.
• Immunoglobulins function by binding to antigens and inactivates them.
 • By complexing with antigens, immunoglobulins create immunoprotein- antigen
complexes that can be recognized and destroyed through reactions with either
complement proteins or cytokines.

TRANSPORTERS
• Transport proteins are a diverse group of proteins that combine with other substances
to provide a means of carrying those substances in the blood, or into cells, or out of
cells, or within cells.
• Transport proteins in cell membranes, for example, carry and thus regulate the flow of
nutrients into and out of cells.
• Several types of transporters exist in cell membranes.
• Some transporters (called uniporters) carry only one substance across cell membranes;
other transporters (called symporters) carry more than one substance.
•
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Antiporters, another type of cell membrane protein transporter, function by
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exchanging one substance for another.
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• For example, the Na+, K+-ATPase pump transports three sodium ions out of the cell
in exchange for two potassium ions, which enter the cell.
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• The protein haemoglobin, found in red blood cells, transports oxygen and carbon
dioxide.
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• Albumin, which transports a variety of nutrients such as calcium, zinc, and vitamin
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B6
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• Transthyretin (also called prealbumin), which complexes with another protein, retinol
binding protein, to transport retinol (vitamin A)
• Transferrin, an iron transport protein
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• Ceruloplasmin, a copper transport protein

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• Lipoproteins, which transport lipids in the blood

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BUFFERS
• Proteins, because of their constituent amino acids, can serve as a buffer in the body
and thus help to regulate acid base balance.
• The pH of the blood and other body tissues must be maintained within an appropriate
range.
 • Blood pH ranges from about 7.35 to 7.45, whereas cellular pH levels are often more
acidic.
• For example, the pH of red blood cells is about 7.2, and that of muscle cells is about
6.9.
• The H+ concentration within cells is buffered by both the phosphate system and the
amino acids in proteins.
• The protein haemoglobin, for example, functions as a buffer in red blood cells.
• In the plasma and extracellular fluid, proteins and the bicarbonate system serve as
buffers.
• Amino acids act as acids or bases in aqueous solutions such as those in the body by
releasing and accepting hydrogen ions, thereby contributing to the buffering capacity
of proteins in the body.

FLUID BALANCERS
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• In addition to acid-base balance, proteins (along with other factors) influence fluid
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balance.
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• The presence of protein in the blood and in cells helps maintain fluid balance, or
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stated differently, helps attract water and contribute to osmotic pressure.

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• Loss of or diminished concentrations of proteins, such as albumin, in the blood

plasma results in a decrease in plasma osmotic pressure.
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• When protein concentrations in the blood are less dense than normal, fluid “leaks” out
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of the blood and into interstitial spaces, causing swelling (edema).

• Restoring adequate protein in the blood (for example, by infusing albumin
intravenously) promotes diffusion of water from the interstitial space back into the
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blood.
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OTHER ROLES
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• Proteins carry out many additional roles.

• For example, in cell membranes, proteins function in cell adhesion, and some further
serve to transmit signals into and out of the cell.
• Proteins also serve as receptors on cell membranes.
• Proteins can function in storage roles.
• For example, some minerals like copper, iron, and zinc are stored in body tissues
bound to proteins; these proteins are often called metalloproteins.
• Many proteins in the body are known as conjugated proteins.
• Conjugated proteins are proteins that are joined to nonprotein components.
• These conjugated proteins have many diverse roles in the body.
• Mucus, which is found in body secretions, is rich in glycoproteins.
• Mucus both lubricates and protects epithelial cells in the body.
• Glycoproteins serve structural roles in connective tissue such as collagen and elastin,
and in bone matrix.
• Some of the body’s hormones, such as thyrotropin, are glycoproteins.

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