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Porter/Edelman
determined basic Ig structure, nobel prize in 1972
Pepsin Digestion
F(ab’)2 and Fc fragments
Papain Digestion
Fc, and two Fab fragments
Mercapoethanol Reduction
Two heavy and two light chains
N-terminus
Found in the variable region of the antibody
C-terminus
Found in the constant region of the antibody
Hinge region
Region where Fab and Fc fragments meet, creates “bend” with prolines and cysteines
Disulfide linkages
Stabilize connections between hinge region, CH1 and CL
Complementary Determining Region (CDR)
most variable region of light and heavy chains, with CDR3 being the most variable that forms the antigen binding site
kappa and lambda
Light chain constants (3 combinations)
mew, gamma, alpha, delta, or epsilon
Heavy chain constants
Light chain variability
About ½ variable acids
Heavy chain variability
About ÂĽ variable acids
Carbohydrate side chain
Found on antibody IgA, IgD, and IgG CH2 domains and IgE and IgM CH3 domains to facilitate solubility
IgG
most abundant Ab in serum, protects fetus, has hinge region
IgM
produced in primary Ag response, forms a pentamer
IgA
main Ab in secretions (milk, saliva, tears, mucous), has hinge region, forms dimer or tetramer in secretions
IgE
contributes to hypersensitivity by binding to Fc receptors on mast cells and basophils to induce histidine and serotonin
IgD
major membrane Ig along with membrane-bound IgM expressed by mature B-cells, has hinge region
IgG3
contains the longest C-chain of the 4 subclasses of the IgG class
Anti-isotype Antibody
made against foreign Ab C-regions (either heavy or light chains)
mIgM
expressed by immature pre-B cells
mIgM and mIgD
expressed by naive, fully mature unstimulated B-cells