HEMOGLOBIN AND MYOGLOBIN

HEMOGLOBIN

 Hemoglobin (Hb) is the red blood pigment, exclusively

found in erythrocytes
 Hemoglobin performs two important biological functions
concerned with respiration
 Delivery of O2 from the lungs to the tissues.
 Transport of CO2 and protons from tissues to lungs for
excretion.
 Structure of hemoglobin
 Hemoglobin (mol. wt. 64,450) is a conjugated protein,
containing globin—the apoprotein part—and the heme—the
non-protein part (prosthetic group)
 Hemoglobin is a tetrameric allosteric protein
 Globin consists of four polypeptide chains of two different
primary structures
 The common form of adult hemoglobin (HbA1) is made up of
two α-chains and two β-chains (α2β2)
 Each α -chain contains 141 amino acids while β -chain contains
146 amino acids.
 Thus HbA1 has a total of 574 amino acid residues.
 The four subunits of hemoglobin are held together by non-
covalent interactions primarily hydrophobic, ionic and
hydrogen bonds.
 Each subunit contains a heme group.
 Structure of heme

 The characteristic red colour of hemoglobin (ultimately blood)

is due to heme.
 Heme contains a porphyrin molecule namely protoporphyrin
IX, with iron at its center.
 Protoporphyrin IX consists of four pyrrole rings to which four
methyl, two propionyl and two vinyl groups are attached
 Other forms of hemoglobin

▪ In adults a small fraction (< 5%) of hemoglobin, known as HbA2 is present.

▪ HbA2 is composed of two α and two δ (delta) chains.
▪ Fetal hemoglobin (HbF) is synthesized during the fetal development and a little of it may be present even in adults.
▪ Glycosylated hemoglobin (HbA1c), formed by covalent binding of glucose is also found in low concentration.
▪ It is increased in diabetes mellitus which is successfully utilized for the prognosis of these patients
 Myoglobin
 Myoglobin (Mb) is monomeric oxygen binding hemoprotein
found in heart and skeletal muscle.
 It has a single polypeptide (153 amino acids) chain with heme
moiety.
 Myoglobin (mol.wt. 17,000) structurally resembles the
individual subunits of hemoglobin molecule.
 For this reason, the more complex properties of hemoglobin
have been conveniently elucidated through the study of
myoglobin.
 Myoglobin functions as a reservoir for oxygen. It further
serves as oxygen carrier that promotes the transport of
oxygen to the rapidly respiring muscle cells.
 Oxygen dissociation curve
Functions of hemoglobin
• Hemoglobin is largely responsible for the transport of O2
from lungs to tissues.
• It also helps to transport CO2 from the tissues to the lungs.

Cooperative binding of O2 to hemoglobin

• The oxygen dissociation curve for hemoglobin is

sigmoidal in shape
• This indicates that the binding of oxygen to one heme
increases the binding of oxygen to other hemes.
• Thus the affinity of Hb for the last O2 is about 100 times
greater than the binding of the first O2 to Hb.
• This phenomenon is referred to as cooperative binding of
O2 to Hb or simply heme-heme interaction. • It is evident from the graph that myoglobin has
• On the other hand, release of O2 from one heme much higher affinity for O2 than hemoglobin.
facilitates the release of O2 from others. • Hence O2 is bound more tightly with myoglobin
• In short, there is a communication among heme groups in than with hemoglobin.
the hemoglobin function. • Further, pO2 needed for half saturation (50%
binding) of myoglobin is about 1 mm Hg
compared to about 26 mm Hg for hemoglobin.
T and R forms of hemoglobin

The four subunits (α2β2) of hemoglobin are held together by weak forces. The relative
position of these subunits is different in oxyhemoglobin compared to deoxyhemoglobin.

R-form of Hb : The binding of O2 destabilizes

T-form of Hb : The deoxy form of
some of the hydrogen and ionic bonds
hemoglobin exists in a T or taut (tense)
particularly between αβ dimers.This results in a
form. The hydrogen and ionic bonds limit
relaxed form or R-form of Hb wherein the
the movement of monomers. Therefore,
subunits move a little freely. Therefore, the R-
the T-form of Hb has low oxygen affinity.
form has high oxygen affinity.
ANTIGEN-ANTIBODY INTERACTION
 • The interaction between an antigen and
an antibody is considered
complementary due to the specific
recognition and binding that occurs
between the two molecules.
• This interaction is highly precise,
resembling a lock-and-key mechanism,
where the unique shape of the antigen
fits into the binding site of the antibody.

The complementary interaction between an antigen and an antibody involves several key aspects

Specificity:
Each antibody is produced
by B cells in response to a
specific antigen.
The binding between the
antigen and the antibody is
highly specific, based on the
specific three-dimensional
structure of the antigen and
the corresponding binding
site (paratope) on the
antibody.
Affinity:
The strength of the
interaction between an
antigen and an antibody is
known as affinity.
It refers to how tightly the
antigen binds to the
antibody's binding site. High
affinity ensures a strong and
stable interaction between
the two molecules.
Recognition
Diversity:
of epitopes:
The immune system can
Antigens can have multiple
generate a diverse
epitopes, which are specific
repertoire of antibodies
regions that can be
capable of recognizing and
recognized by the binding
binding to a wide range of
sites of different antibodies.
antigens.
This enables the immune
This diversity allows the
system to target various
immune system to combat
parts of a pathogen or
various pathogens and
foreign substance, enhancing
foreign substances
the overall efficacy of the
effectively.
immune response