Antibody structure Flashcards
Region of the antibody molecule that provides flexibility for multiple binding sites
Hinge region
Type of bonds joining the heavy and light chains in an antibody molecule
Disulfide bonds
Antibody molecule structure with 2 identical light chains and 2 identical heavy chains
Monomer
Designation of heavy chains in different antibody classes
μ (IgM), δ (IgD), γ (IgG), α (IgA), ε (IgE)
Number of constant domains in a heavy chain
Three (CH1, CH2, CH3)
Domain of the heavy chain responsible for antigen specificity
Variable domain (VH)
Designation of light chains
Kappa (κ) and Lambda (λ)
Ratio of kappa to lambda light chains
‘2:1
Number of domains in a light chain
One constant domain (CL) and one variable domain (VL)
Part of the antibody containing antigen-binding sites
Variable regions at the end of the Y arms
Location of the hinge region in the antibody
Between CH1 and CH2 domains
Properties of antibodies
Protein in nature, high molecular weight (>150,000 daltons), present in serum, CSF, saliva, and seminal fluid
Weight of the heavy chain in daltons
50,000-90,000 daltons
Weight of the light chain in daltons
Approximately 23,000 daltons
Number of amino acid residues in the kappa light chain
214 amino acids
Number of amino acid residues in the lambda light chain
213 amino acids
Region of the antibody that remains consistent and contributes to structure
Constant region
Region of the antibody that varies and determines antigen specificity
Variable region
Cell stage where heavy chain gene rearrangement begins
Pro-B cell stage on chromosome 14
Antigenic differences in constant heavy regions of antibodies; determines Ig class
Isotypes
Additional antigenic features of Ig that vary among individuals; variation in the constant region of both HC and LC
Allotypes
Antigenic determinants formed by specific amino acids in hypervariable regions
Idiotypes