CENTURION UNIVERSITY OF TECHNOLOGY AND MANAGEMEN
Immunoglobulins
Presente
Ms. Swati
Teaching
School o
CUTM, P
,Immunoglobulins
• Immunoglobulins are Y-shaped proteins produced by plasma cells
(differentiated B-lymphocytes) that specifically bind to antigens, su
as bacteria, viruses, or toxins, to neutralize them or mark them for
destruction. They are a key component of the adaptive immune
system, providing specificity and memory to immune responses.
Immunoglobulins are found in blood, tissue fluids, and mucosal
secretions, and their structure enables diverse functions, from
pathogen neutralization to immune regulation.
, Structure of Immunoglobulins
The structure of immunoglobulins is highly conserved across their
classes, consisting of polypeptide chains organized into functional
domains. The basic structure is a monomeric unit, with variations in
multimeric forms for certain classes.
1. Basic Structural Unit
• Composition: Each immunoglobulin monomer consists of four
polypeptide chains:
• Two Heavy Chains (H): Approximately 50-70 kDa each, determining the
immunoglobulin class.
• Two Light Chains (L): Approximately 25 kDa each, contributing to antigen binding.
• Chain Linkage: The chains are linked by disulfide bonds and non-
covalent interactions, forming a Y-shaped molecule.
• Domains: Each chain is organized into immunoglobulin domains (110-
120 amino acids), stabilized by intrachain disulfide bonds:
• Heavy chains: 4-5 domains (VH, CH1, CH2, CH3, and CH4 in some classes).
• Light chains: 2 domains (VL and CL).
Immunoglobulins
Presente
Ms. Swati
Teaching
School o
CUTM, P
,Immunoglobulins
• Immunoglobulins are Y-shaped proteins produced by plasma cells
(differentiated B-lymphocytes) that specifically bind to antigens, su
as bacteria, viruses, or toxins, to neutralize them or mark them for
destruction. They are a key component of the adaptive immune
system, providing specificity and memory to immune responses.
Immunoglobulins are found in blood, tissue fluids, and mucosal
secretions, and their structure enables diverse functions, from
pathogen neutralization to immune regulation.
, Structure of Immunoglobulins
The structure of immunoglobulins is highly conserved across their
classes, consisting of polypeptide chains organized into functional
domains. The basic structure is a monomeric unit, with variations in
multimeric forms for certain classes.
1. Basic Structural Unit
• Composition: Each immunoglobulin monomer consists of four
polypeptide chains:
• Two Heavy Chains (H): Approximately 50-70 kDa each, determining the
immunoglobulin class.
• Two Light Chains (L): Approximately 25 kDa each, contributing to antigen binding.
• Chain Linkage: The chains are linked by disulfide bonds and non-
covalent interactions, forming a Y-shaped molecule.
• Domains: Each chain is organized into immunoglobulin domains (110-
120 amino acids), stabilized by intrachain disulfide bonds:
• Heavy chains: 4-5 domains (VH, CH1, CH2, CH3, and CH4 in some classes).
• Light chains: 2 domains (VL and CL).
