Antibody Structure Flashcards
H chain
heavy chain, MW=50,000, each antibody has 2 H chains, each H chain has 1 variable domain (VH) and 3-4 constant domains (CH1, CH2, CH3, (CH4)), 5 kinds of H chains (gamma, alpha, mu, epsilon, delta—each corresponds to the appropriately named antibody: IgA has alpha chains
L chain
light chain, MW= 25,000, each antibody has 2 L chains, each L chain has 1 variable domain (VL) and 1 constant domain (CL)
kappa and lambda chains
2 varieties of L chain, each cell that makes antibody has a choice, but it uses only one kind.
hinge region
allows for flexibility so that when bound to antigen, the constant part of the antibody can change conformation
Fab
S–S bonds between the H chains fully reduced
F(ab2)
2 Fabs still joined by S—S bond
Fc
non-antigen binding region of the antibody, makes antibody participate in complement
complementarity-determining regions (hypervariable regions)
light chain and heavy chain variable region is NOT uniformly variable, most of the variability is in 3 regions called hyper-variable regions of CDR’s, amino acids in this region comprise the actual antigen-binding site
variable (V) and constant (C) domains,
- variable (V) domain: at N-terminal of antibody, differences in amino acid sequences between antibodies of different specificities
- constant (C) domains: region that is essentially identical on the antibodies, made up of 1 (in L chains and 4 (in epsilon and mu) compact, structurally similar domains called C domains.
VL and CL
variable domain of light chain and constant domain of light chain
VH and CH
variable domain of heavy chain and constant domain of heavy chain
Diagram an electrophoretic separation of human, label the anode and cathode, and identify the albumin, alpha 1, alpha 2, beta and gamma peaks.
diagram this
Name the 5 antibody classes, and their characteristic heavy chains.
a. IgG: 2 light and 2 gamma (heavy) chains
b. IgE: 2 light and 2 epsilon (heavy) chains
c. IgD: 2 light and 2 delta (heavy) chains
d. IgA: 4 light, 4 alpha (heavy) chains, 1 Joining chain and 1 Secretory component
e. IgM: 10 light, 10 mu and 1 joining chain
Draw a diagram of the structure of typical molecules of each class, and label the heavy and light chains; Fc and Fab parts; J chains if any; antibody combining sites; main interchain disulfide bonds; and secretory component
Draw this
Distinguish the 5 immunoglobin classes in terms of size, and for IgG, IgM and IgA, their approximate concentration of serum.
G: 150,000, serum = 1000 mg/dL E: 190,000 D: 180,000 A: 400,000, serum = 200 mg/dL M: 900,000, 100 mg/dL