Antibody Structure Flashcards

1
Q

H chain

A

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

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2
Q

L chain

A

light chain, MW= 25,000, each antibody has 2 L chains, each L chain has 1 variable domain (VL) and 1 constant domain (CL)

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3
Q

kappa and lambda chains

A

2 varieties of L chain, each cell that makes antibody has a choice, but it uses only one kind.

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4
Q

hinge region

A

allows for flexibility so that when bound to antigen, the constant part of the antibody can change conformation

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5
Q

Fab

A

S–S bonds between the H chains fully reduced

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6
Q

F(ab2)

A

2 Fabs still joined by S—S bond

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7
Q

Fc

A

non-antigen binding region of the antibody, makes antibody participate in complement

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8
Q

complementarity-determining regions (hypervariable regions)

A

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

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9
Q

variable (V) and constant (C) domains,

A
  • 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.
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10
Q

VL and CL

A

variable domain of light chain and constant domain of light chain

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11
Q

VH and CH

A

variable domain of heavy chain and constant domain of heavy chain

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12
Q

Diagram an electrophoretic separation of human, label the anode and cathode, and identify the albumin, alpha 1, alpha 2, beta and gamma peaks.

A

diagram this

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13
Q

Name the 5 antibody classes, and their characteristic heavy chains.

A

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

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14
Q

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

A

Draw this

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15
Q

Distinguish the 5 immunoglobin classes in terms of size, and for IgG, IgM and IgA, their approximate concentration of serum.

A
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
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16
Q

Describe the structure of antibody combining sites.

A

Combining site is where the antibody binds to the antigen, is made up of V domains of both the H and L chain (VH and VL)

17
Q

Explain why complementarity-determining regions are also called hypervariable regions.

A

There are 3 hyper variable regions on the variable domain of light and heavy chains. These regions have amino acid variability. It is more functionally significant to call them complementarity-determining

18
Q

Give an example of an allotype

A

minor allelic differences in the sequence of immunoglobulins between individuals, determined by allotypes of your parents, useful in determining relatedness

19
Q

Give an example of a subclass

A

immunoglobulins are divided into subclasses because of slight differences in the amino acid sequences of their H chain C regions. IgG1, IgG2, IgG3, IgG4. IgA1, IgA2. IgM1, IgM2. IgD and IgE.

20
Q

Give an example of an idiotype

A

unique combining region, made up of the CDR amino acids of its L and H chain, that each antibody has. Anti-idiotype: antibodies made that recognize the unique sequence of that combining site.