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
Unique differences between antibodies of different antigen binding specificities
Idiotypes
Warm-reacting antibody in the blood
IgG
Immunoglobulin that provides immunity for the newborn
IgG
Immunoglobulin that is the only antibody that can cross the placenta
IgG
Immunoglobulin class best known for complement activation via the classical pathway
IgG
Subclasses of IgG best for placental transfer
IgG1
Subclass of IgG best in activating complement
IgG3
Subclass of IgG with no participation in complement fixation
IgG4
Immunoglobulin that participates in opsonization, neutralizing toxins, and viruses
IgG
Type of bonds involved in differentiating IgG subclasses
Disulfide bonds
Subclass of IgG with the longest disulfide bonds
IgG3
Largest immunoglobulin
IgM
Major antibody class secreted in the early stages of a primary antibody response
IgM
Form of IgM with 10 antigen-binding sites
Pentameric IgM
First class of antibody produced by developing B cells
IgM
Best complement fixer antibody
IgM
Antibody class that causes agglutination
IgM
Immunoglobulin found in serum as pentamer and on B cells as monomer
IgM
Major antibody on mucosal surfaces
IgA
Immunoglobulin associated with anaphylaxis
IgA
Serum structure of IgA
Monomer type I
Structure of secretory IgA
Dimer with secretory component
Immunoglobulin with anti-inflammatory properties
IgA
Chain that transfers secretory IgA to secretions
J chain
Protein that prevents enzymatic degradation of secretory IgA
Secretory protein
Immunoglobulin involved in immunoregulation
IgD
Immunoglobulin found on the surface of B cells
IgD
Major membrane immunoglobulin on mature B cells
IgM and IgD
Immunoglobulin found on immature B cells
IgM
Postulated function of IgD
Anti-idiotypic antibody
Heat-labile antibody involved in allergic reactions
IgE
Antibody that attaches to human skin and initiates allergic reactions
IgE
Type of antibody involved in type I hypersensitivity reaction
IgE
Cells that IgE has affinity to
Basophils and mast cells
