SAMSON, Glydel Mae T.

BMLS 2-1
BIOCHEMISTRY OF PROTEINS

Characteristics of Protein

All proteins contain the elements carbon, hydrogen, oxygen, and nitrogen.
Presence of nitrogen in proteins sets them apart from carbohydrates and lipids, which most often do
not contain nitrogen.
Average nitrogen content of proteins = 15.4% by mass.
protein - naturally occurring, unbranched polymer in which the monomer units are amino acids
Protein= proteios (greek) - of first importance. This reflects the key role that proteins play in life
processes.

Amino acids: The Building Blocks for Proteins

◇Amino Acid
▪︎ An organic compound that contains both an amino (-NH2) group and a carboxyl (-COOH) group.
▪︎ Amino acids found in proteins are always a-amino acids
▪︎ A-amino acid is an amino acid in which the amino acid group and the carboxyl group are attached to the
a-carbon atom.

The R group present in an o-amino acid is called amino acid side chain
The nature of this side chain distinguishes a-amino acids from each other
Side chains vary in size, charge, acidity, functional groups present, hydrogen bonding ability, and
chemical reactivity

Amino acids are grouped according to side chain polarity.

four categories
(1) Nonpolar amino acids
(2) Polar neutral amino acids
(3) Polar acidic amino acids
(4) Polar basic amino acids

◇ Nonpolar amino acid

▪︎Amino acid that contains one amino group, one carboxyl group, and a nonpolar side chain
▪︎When incorporated into a protein, such amino acids are hydrophobic, not attracted to water
▪︎Tryptophan is borderline member of this group because water can weakly interact through hydrogen
bonding with the NH ring location on tryptophan's side-chain ring structure
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◇ Polar neutral amino acid

▪︎Amino acid that contains one amino group, one carboxyl group, and a side
chain that is polar but neutral
▪︎The side chain of a polar neutral amino acid is neither acidic nor basic
▪︎more soluble in water than the nonpolar amino acids as, in each case, the R
group present can hydrogen-bond to water

◇ Polar acidic amino acid

▪︎Amino acid that contains one amino group, and two carboxyl group, the second
carboxyl group being part of the side of chain
▪︎The side chain of a polar acidic amino acid bears negative charge; the side chain
has lost its acidic hydrogen atom

◇ Polar basic amino acid

▪︎Amino acid that contains two amino group, and one carboxyl group, the second amino group being part of
the side of chain
▪︎The side chain of a polar basic amino acid bears positive charge; the nitrogen atom has accepted a proton

All of the standard amino acids are necessary constituents of human proteins Adequate
amounts of 11 of the 20 standard amino acids can be synthesized from carbohydrates and lipids
in the body if a source of nitrogen is also available
The adult human body cannot produce adequate amounts of the other nine standard amino
acids
These amino acids, which are called essential amino acids, must be obtained from dietary
protein
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◇ Essential amino acids

▪︎ A standard amino acid needed for protein synthesis
that must be obtained from dietary sources because the
human body cannot synthesize it inadequate amounts
from other substances

◇ Peptides
▪︎ Amino acids can bond together to produce an unbranched chain
of amino acids
Length of amino acid chain can vary from a few amino acids to
many amino acids
such a chain of covalently linked amino acids is called a peptide
Peptide is an unbranched chain of amino acids
a compound containing 2 amino acids is specifically called
dipeptide
3 amino acids joined together in a chain constitute a tripeptide
oligopeptide- used to refer to peptides with 10-20 amino acids
residues
polypeptide- to longer peptides; long unbranched chain of
amino acids

Biochemically imprtant small peptides

Small Peptide Hormones

The two best-known peptide hormones, both produced by the pituitary gland, are oxytocin and vasopressin.
◇ Oxytocin
▪︎regulates uterine contraction and lactation
◇ Vasopressin
▪︎regulates the excretion of water by kidneys; it also affects blood pressure
▪︎Antidiuretic hormone (ADH) is another name for vasopressin - this name relates to vasopressin's function in
the kidneys, which is to decrease water elimination from the body

Small Peptide Neurotransmitters

◇ Enkephalins
▪︎Pentapeptide neurotransmitters produced by the brain itself that bind at receptor sites in the brain to
reduce pain
▪︎The two best-known enkephalins are Mot-enkephalin and Lou-enkephalin

Small Peptide Antioxidants

◇ Glutathione
▪︎Present in significant concentrations in most cells and is considerable physiological importance as a
regulator of oxidation-reduction reactions.
▪︎ Protects cellular contents from oxidizing agents as proxides and superoxides.
◇ Protein
▪︎A peptide in which at least 40 amino acid residues are present.
▪︎The terms polypeptide and protein are often used interchangeably; a protein is a relatively long
polypeptide
▪︎The key point is that the term protein is reserved for peptides with a large number of amino acids; it is not
correct to call a tripeptide a protein
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General Structural Characteristics of Proteins

Monomeric and Multimeric Proteins

◇Monomeric proteins
▪︎ A protein in which only one peptide chain is present
◇Multimeric proteins
▪︎ A protein in which more than one peptide chain is present
▪︎The peptide chains present in multimaric proteins are called protein subunits

Simple and Complex Proteins

◇Simple Protein
▪︎A protein in which only amino acid residues are present
▪︎More than one protein subunit may be present in a simple protein, but all subunits contain only
amino acids

◇Conjugated proteins
▪︎ A protein that has one or more non-amino-acid entities present in its structure in addition to one or
more peptide chains
▪︎The non-amino-acid components present in a conjugated protein, which may be organic or inorganic,
are called prosthetic groups
▪︎Prosthetic group is a non-amino-acid group present in a conjugated protein

4 STRUCTURAL LEVELS OF PROTEIN:

◇ Primary Structure
◇ Secondary Structure
◇ Tertiary Structure
◇ Quaternary Structure

◇ Primary Structure
▪︎The order in which amino acids are linked together in a protein
▪︎ Always involves more than just the numbers and kinds of amino acids present; it also involves the order of
attachment of the amino acids to each other through peptide bonds
▪︎The primary structure of a specific protein is always the same regardless of where the protein is found within an
organism. The structures of certain proteins are even similar among different species of animals

◇ Primary protein structure

▪︎ Insulin, the hormone that regulates blood glucose levels, was the first protein for which primary
structure was determined
▪︎ The sequencing of its 51 amino acids was completed in 1953, after eight years of work by the British
biochemist Frederick Sanger
▪︎The primary structures of insulin in cows, pigs, sheep, and horses are very similar both to each other and
to human insulin.
Such similarity was important for diabetics who required supplemental injections of insulin
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◇ Secondary Structure
▪︎ The arrangement in space adopted by the backbone portion of a protein
▪︎ The two most common types of secondary structure are the alpha helix (a helix) and the beta pleated (ẞ pleated)
sheet.

◇ Secondary Protein Structure

▪︎The Alpha Helix
A protein secondary structure in which a single protein chain adopts
a shape that resembles a coiled spring (helix), with the coil
configuration maintained by hydrogen bonds

◇ Tertiary Structure
▪︎The overall three-dimentional shape of a protein that results from the
interactions between amino acid side chains that are widely separated from
each other within a peptide chain
▪︎ Four stabilizing interactions contribute to the tertiary structure of a
protein:
1. Covalent disulfide bonds
2. Electrostatic attractions
3. Hydrogen bonds
4. Hydrophobic attractions

◇ Quaternary Structure
▪︎The highest level of protein organization
▪︎It is found only in multimeric proteins - such proteins have structures involving two or more peptide subunits
that are independent of each other- that is, are not covalently bonded to each other.
▪︎An example of a protein with quaternary structure is hemoglobin, the oxygen- carrying protein in blood. It is
tetramer in which there are two identical a subunits and two identical ẞ subunits. Each subunits enfolds a heme
group, the site where oxygen binds to protein.

• Protein Denaturation
▪︎ The partial or complete disorganization of a protein's characteristic three- dimentional shape as a result of
disruption of its secondary, tertiary, and quaternary structural interactions
▪︎ Because the biochemical function of a protein depends on its three- dimentional shape, the result of denaturation
is loss of biochemical activity
▪︎Protein denaturation does nor affect the primary structure of a protein

▪︎ example of protein denaturation occurs when egg white a

concentrated solution of the protein albumin) is poured
onto a hot surface.
▪︎ The clear albumin solution immediately changes into a
white solid with a jellylike consistency

• Protein Renaturation
▪︎ Often, for limited denaturation changes, it is possible to find conditions under which the effects of denaturation
can be reversed.
▪︎ This restoration, process in which the protein is "refolded", is called renaturation
▪︎However, for extensive denaturation changes, the process is usually irreversible.
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• Protein Hydrolysis
▪︎ When protein or smaller peptide in a solution of strong base is heated, the peptide bonds of the amino acid chain
are hydrolyzed and free amino acids are produced
▪︎ The hydrolysis reaction is the reverse of the formation reaction for peptide bond
▪︎Complete hydrolysis - all peptide bonds are broken freeing up all of the constituent amino acids; amino acids are
the only products
▪︎Partial hydrolysis - some, but not all, of the peptide bonds are broken producing a product mixture that contains
both free amino acids and small peptides.

Protein Classification Based on Shape

▪︎Based on molecular shape, which is determines primarily by tertiary and quaternary structural features, there are
three main types of protein:
▪︎Fibrous protein - protein whose molecules have an elongated shape with one dimension longer
than others
▪︎Globular protein - protein whose molecules have peptide chains that are folded into spherical or
globular shapes
▪︎Membrane protein - protein that is found associated with a membrane system of a cell

Fibrous proteins
◇a-Keratin
-Major protein constituent of hair, feathers, wool, fingernails, claws, scales, horns, turtle shells, quills, and hooves
◇Collagen
-Most abundant of all proteins in humans (30% of total body protein)
-Major structural material in tendons, ligaments, blood vessels, and skin; it is also the organic component of
bones and teeth

Globular proteins
◇Hemoglobin
-Transports oxygen from lungs to tissue
-It is a tetramer (four peptide units) with each subunit also containing a heme group, the entity that binds oxygen
-With four heme groups present, a hemoglobin molecule can transport four oxygen molecules at the same time
◇Myoglobin
-Functions as an oxygen-storage molecule in muscles
-Consists of a single peptide chain and a heme unit, thus only one oxygen molecule can be carried by a
myoglobin molecule
-Has higher affinity for oxygen than does hemoglobin
-Oxygen stored in myoglobin molecules serves as a reserve oxygen source for working muscles when their
demand for oxygen exceeds that which can be supplied by hemoglobin
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Protein Classification Based on Function

◇Catalytic proteins
-Proteins are probably best known for their role as catalysts
-Proteins with the role of biochemical catalyst are called enzymes
-Enzymes participate in almost all of the metabolic reactions that occur in cells

◇Defense proteins
-These proteins are, also called immunoglobulins or antibodies, are central to the functioning of the body's
immune system
-They bind to foreign substances, such as bacteria or viruses, to help combat invasion of the body by foreign
particles

◇Transport proteins
-These proteins bind to particular small biomolecules and transport them to other locations in the body and
then release the small molecules as needed at the destination location
Example: hemoglobin, transferrin, lipoproteins

◇Messenger proteins
-These proteins transmit signals to coordinate biochemical processes between different cells, tissues, and
organs
Example: hormones like insulin and glucagon, human growth hormone

◇Contractile proteins
-These proteins are necessary for all forms of movement
-Muscles are composed of filament-like contractile proteins that, in response to nerve stimuli, undergo
conformation changes that involve contraction and extension; actin and myosin are example of such proteins

◇Structural proteins
-These proteins confer stiffness and rigidity to otherwise fluid-like biochemical systems
Example: collagen - a component of cartilage

◇Transmembrane proteins
.
-These proteins, which span a cell membrane, help control the movement of small molecules and ions through
the cell membrane
-Many such proteins have channels trough which molecules can enter and exit a cell

◇Storage proteins
-These proteins bind (and store) small molecules for future use
-During degradation of hemoglobin, the iron atoms present are released and become part of ferritin, an iron-
storage protein, which saves the iron for use in the biosynthesis of new hgb molecules

◇Regulatory proteins
-These proteins are often found embedded in the exterior surface of cell membranes
-They act as sites at which messenger molecules, including messenger proteins such as insulin, can bind and
thereby initiate the effect that the messenger carries

.◇Nutrient proteins
-These proteins are particularly important in the early stages of life, from embryo to infant
-Casein, found in milk, nourish and provide immunological protection; three- fourths of the protein in milk is
casein

.
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◇Buffer proteins
-These proteins are part of the system by which the acid-base balance within body fluids is maintained
-Transmembrane proteins regulate the movement of ions in and out of cells, ensuring that ion concentration are
those needed for correct acidity/alkalinity

◇Fluid-balance proteins
-These proteins help maintain fluid balance between blood and surrounding tissue
-Albumin and globulin are two well-known fluid-balance proteins found in the capillary beds of the circulatory
system

.
Glycoproteins

◇Glycoprotein
-A protein that contains carbohydrates or carbohydrate derivative in addition to amino acids.
-The carbohydrate content of glycoproteins is variable, but it is fixed for any specific glycoproteins.

◇Collagen
-The presence of carbohydrate units (mostly glucose, galactose, and their
disaccharides) attached to glycosidic linkages to collagen at its 5-hydrolysine
residues causes collagen to be classified as a glycoprotein
-The function of the carbohydrate groups in collagen is related to cross-linking;
they direct the assembly of collagen triple helices into more complex aggregations
called collagen fibrils

◇Immunoglobulins
-A glycoprotein produced by an organism as a protective response to
the invasion of microorganisms or foreign molecules
-Different classes of immunoglobulins, identified by differing
carbohydrate
content and molecular mass, exist.
-Serve as antibodies to combat invasion of the body by antigens
-Antigen a foreign substance, such as a bacterium or virus, that
invades the human body
-Antibody a biochemical molecule that counteracts a specific antigen

All types of immunoglobulin molecules have much the same basic

structure, which includes the following features:
1. Four polypeptide chains are present: two identical heavy (H) chains
and two identical light (L) chains.
2. The H chains, which usually contain 400-500 amino acid residues,
is approximately twice as long as the L chains
3. Both the H and L chains have constant and variable regions. The
constant regions have the same amino acid sequence in each
immunoglobulin.
4. The carbohydrate content of various immunoglobulins varies from
1% to 12% by mass.
5. The secondary and tertiary structures are similar for all
immunoglobulins. They involve a Y- shaped conformation with
disulfide linkages between H and L chains stabilizing the structure.
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Lipoproteins

◇Lipoprotein
- A conjugated protein that contains lipids in addition to amino acids
-The major function of such proteins is to help suspend lipids and transport them through the bloodstream

◇Plasma lipoprotein
-A that is involved in the transport system for lipids in the bloodstream
-These proteins have a spherical structure that involves a central core of lipid material (triacylglycerols and
cholesterol esters) surrounded by a shell (membrane structure) of phospholipids, cholesterol, and proteins

1. Chylomicrons
-Their function is to transport dietary triacylglycerols from intestine to the liver and to adipose
tissue.

2. Very-low-density lipoproteins (VLDLs)

-Their function is to transport triacylglycerols synthesized in the liver to adipose tissue.

3. Low-density lipoproteins (LDLs)

-Their function is to transport cholesterol synthesized in the liver to cells throughout the body.

4. High-density lipoproteins (HDLs)

-Their function is to collect excess cholesterol from body tissues and transport it back to the liver for
degradation to bile acids.

PROTEIN METABOLISM

Protein Digestion and Absorption

-Protein digestion begins in the stomach rather than in the mouth because saliva contains no enzymes that
affect proteins.
-Both protein denaturation and protein hydrolysis occur in the stomach.
-The partially digested protein passes from the stomach into the small intestine, where digestion is completed.
-Dietary protein entering the stomach effects the release of the hormone gastrin by stomach mucosa cells.
-Gastrin's presence causes both hydrochloric acid and pepsinogen secretion.

◇Hydrochloric acid has three major functions within the stomach:

(1) Its antiseptic properties kill most bacterias,

(2) Its denaturing action "unwinds" globular proteins, making peptide bonds more accessible to digestive
enzymes
(3) Its acidity leads to the activation of pepsinogen, which is the in active form of the digestive enzyme pepsin;
because of the hydrochloric acid present, gastric juice has a pH between 1.5 and 2.0

◇Pepsin effects the hydrolysis of approximately 10% of peptide bonds present in proteins,
producing a variety of polypeptides.

Passage, in small batches, of the stomach's acidic protein contents into the small intestine
stimulates production of the hormone secretin, which in turn stimulates pancreatic production
of bicarbonate ion, HCO3, whose function is neutralization of gastric hydrochloric acid.
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With such neutralization, the partially digested protein mix becomes slightly basic, with a pH value between
7.0 and 8.0
This basic environment allows for the production of the pancreatic digestive enzymes trypsin,
chymotrypsin, and carboxypeptidase, all of which attack peptide bonds
Aminopeptidase, secreted by intestinal mucosal cells, also attacks peptide bonds

Pepsin, trypsin, chymotrypsin, carboxypeptidase, and aminopeptidase are all examples of proteolytic
enzymes. Enzymes of this type are produced in inactive forms called zymogens that are activated at their
site of action.

The net result of protein digestion is the release of the protein's constituent amino acids.
Absorption of these "free" amino acids through the intestinal wall requires active transport with the
expenditure of energy.
Different transport systems exist for the various kinds of amino acids. After passing through the intestinal
wall, the free amino acids enter the blood stream, which distributes them throughout the body.

Amino Acid Utilization

Amino acids produced from the digestion of proteins enter the amino acid pool of the body.
The amino acid pool is the total supply of free amino acids available for use in the human body
The amino acid pool is not a specific location within the body where free amino acids "congregate". Rather,
these free amino acids are present throughout the body

Three sources that contributes amino acids to the amino acid pool:
(1) Dietary protein
(2) Protein turnover
(3) Biosynthesis of amino acids in the liver

Protein turnover- repetitive process in which proteins are degraded and resynthesized within the human
body.
Disease, injury, and "wear and tear" are all causes of degradation
Biosynthesis of amino acids by the liver also supplies the amino acid pool with amino acids. However, only
the nonessential amino acids can be produced in this manner.

Nitrogen balance - the state that results when the amount of nitrogen taken into the human body as
protein equals the amount of nitrogen excreted from the body in waste materials

2 types of Nitrogen Imbalance can occur:

Negative nitrogen balance
Positive nitrogen balance

◇Negative nitrogen balance

when protein degradation exceeds protein synthesis, the amount of nitrogen in the urine exceeds the
amount of nitrogen ingested (dietary protein)
This condition accompanies a state of "tissue wasting," because more tissue proteins are being catabolized
than are being replaced by protein synthesis
(1) Protein poor diets,
(2) starvation, and
(3) wasting illnesses

◇Positive nitrogen balance

Nitrogen intake exceeds nitrogen output
The rate of protein anabolism (synthesis) exceeds that of protein catabolism
This state indicates that large amounts of tissue are being synthesized
(1) during growth,
(2) pregnancy, and
(3) convalescence from an emaciating illness
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Amino Acid Utilization

The amino acids from the body's amino acid pool are used in four different ways.

1. Protein Synthesis
It is estimated that about 75% of free amino acids in a healthy, well- nourished adult go into protein
synthesis. Proteins are continually needed to replace old tissue (protein turnover) and also to build new
tissue (growth)

2. Synthesis of nonprotein nitrogen-containing compounds

Amino acids are regularly withdrawn from the amino acid pool for the synthesis of nonprotein nitrogen-
containing compounds such as
-purines and pyrimidines of nucleic acids,
-the heme of hemoglobin,
-the choline and ethanolamine of phosphoglycerides,
-hormones such as adrenaline,
-neurotransmitters such as norepinephrine, dopamine, and serotonin

3. Synthesis of nonessential amino acids

The body draws on the amino acid pool for raw materials for the production of nonessential amino acids
that are in short supply

4. Production of energy
Amino acids in excess of those needed for biosynthetic processes are used as energy sources, being
degraded to substances that can be processed through the common metabolic pathway

In all degradation pathways, the amino nitrogen atom is removed and ultimately is excreted from the body
as urea. The remaining carbon skeleton is then converted to pyruvate, acetyl CoA, or a citric acid cycle
intermediate, depending on its makeup, with the resulting energy production or energy storage

The Urea Cycle

A cyclic biochemical pathway in which urea is produced, for excretion, using ammonium ions and aspartate
molecules as nitrogen sources
The urea
- produced in the liver, transported in the blood to the kidneys and eliminated from the body in urine
- in the pure state, urea is a white solid with a melting point of 133°C
- very soluble in water, is odorless and colorless, and has a salty taste
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The Urea Cycle

◇Steps of the Urea Cycle◇

Step 1: Carbamoyl group transfer

In the mitochondrial matrix, carbamoyl phosphate, upon entering the urea cycle, transfers its carbamoyl
group to ornithine to form citrulline
With the carbamoyl transfer, the first of the two nitrogen atoms and the carbon atom needed for the
formation of urea have been introduced into the cycle

Step 2: Citrulline-aspartate condensation

Citrulline is transported into the cytosol where a condensation reaction between it and aspartate occurs.
Aspartate is the second molecule of "fuel" entering the cycle, having been previously generated from
glutamate by transamination
The condensation, which produces arginosuccinate, is catalyzed by argininosuccinate synthetase

Step 3: Argininosuccinate cleavage

The enzyme argininosuccinate lyase catalyzes the cleavage of argininosuccinate into arginine, a standard
amino acid, and fumarate, a citric acid cycle intermediate

Step 4: Urea from arginine hydrolysis

Hydrolysis of arginine produces urea and regenerates ornithine, one of the cycle's starting materials. The
enzyme involved is arginase
The oxygen atom present in the urea comes from the water involved in the hydrolysis.
The ornithine is transported back into the mitochondria, where it becomes available to participate in the
urea cycle again

Urea Cycle Net Reaction

Four ATP molecules is expended in the production of one urea molecule

■Two ATP molecules are consumed in the production of carbamoyl phosphate
■ Two ATP molecules are consumed in Step 2 of the urea cycle

Urea formed via the urea cycle is excreted in the urine. Urea is one of several molecules eliminated from the
body through urine.
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The Chemical Composition of Urine

On average, about 4 g of solutes are present in a 100-g urine sample

◇The solutes present in urine are of two general types:

(1) Organic compounds
(2) Inorganic ions

The urea is odorless and colorless in solution.

The pale yellow color of urine is due to small amounts of
urobilinogen and related compounds.
The most abundant inorganic constituent is chloride ions. Its
primary source is dietary table salt (NaCl).
The second most abundant ion present is sodium ion, the positive
ion in table salt.
Sulfate ion comes primarily from the metabolism of sulfur-
containing amino acids.
Ammonium ions come primarily from hydrolysis of urea
Urine is normally slightly acidic, having an average ph value of 6.6
Fruits and vegetables in the diet tend to raise urine pH, and high-
protein foods tend to lower urine pH
A normal adult excretes 1000-1500mL of urine daily.

Amino Acid Biosynthesis

The classification of amino acids as essential or nonessential for humans roughly parallels the number of
steps in their biosynthetic pathways and the energy required for their synthesis.
Nonessential amino acids require fewer reaction steps in their biosynthetic pathways than essential amino
acids.
Number of Reaction Steps Required for the Synthesis of Nonessential and Essential Amino Acids:

A summary of the starting materials for the biosynthesis of the 10 non essential amino acids.

Three of the non essential amino acids- alanine, aspartate, and glutamate- are biosynthesized by
transamination of the appropriate a-keto acid starting material.

The nonessential amino acid tyrosine is obtained from the essential amino acid phenylalanine in a one-step
oxidation that involves molecular O2, NADPH, and the enzyme phenylalanine hydroxylase. Lack of this
enzyme causes the metabolic disease phenylketonuria (PKU).
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Hemoglobin Catabolism

RBCs are highly specialized cells whose primary function is to deliver oxygen to, and remove carbon
dioxide, from body tissues.
Mature RBCs have no nucleus or DNA. Instead,they are filled with the red pigment hemoglobin.
RBC formation occurs in the bone marrow, and about 200 billion new red blood cells are formed daily. The
life span of a red blood cell is about four months.
The oxygen-carrying ability of the red blood cells is due to the protein hemoglobin present in such cells.
Hgb is a conjugated protein; the protein portion is called globin, and the prosthetic group (nonprotein
portion) is heme. Heme contains four pyrolle groups joined together with an iron atom in the center.
It is the iron atom in heme that interacts with O₂ forming a reversible complex with it.
Old RBCs are broken down in the spleen (primary site) and liver (secondary site)
Part of this process is degradation of hemoglobin. The globin protein is hydrolyzed to amino acids, which
become part of the amino acid pool. The iron atom of heme becomes part of ferritin, an iron-storage
protein, which saves the iron for use in the biosynthesis of new hemoglobin molecules. The tetrapyrrole
carbon arrangement of heme is degraded to bile pigment that are eliminated in feces and to a lesser extent
in urine.

Bile Pigments

The tetrapyrrole degradation products obtained from heme are known as bile pigments because they are
secreted with the bile, and most of them are highly colored.
A bile pigment is a colored tetrapyrole degradation product present in bile.
-Biliverdin and bilirubin are, respectively, green and reddish-orange in color.
Stercobilin has a brownish hue and is the compound that gives feces their characteristic color.
Urobilin is the pigment that gives urine its characteristic yellow color. • Normally, the body excretes 1-2 mg
of bile pigments in urine daily and 250-350 mg of bile pigments in feces daily.
When the body is functioning properly, the degradation of heme in the spleen to bilirubin and the removal
of bilirubin from the blood by the liver balance each other.
Jaundice is the condition that occurs when this balance is upset such that bilirubin concentrations in the
blood become higher than normal. The skin and the white of the eyes acquire a yellowish tint because of
the excess bilirubin in the blood.
Jaundice can occur as a result of:
1. liver diseases, such as infectious hepatitis and cirrhosis, that decrease the liver's ability to process bilirubin
2.From spleen malfunction, in which heme is degraded more rapidly that it can be absorbed by the liver,
3. From gallbladder malfunction, usually from an obstruction of the bile duct