Chapter 5 Flashcards

1
Q

Serum lacks which blood components?

A

Coagulation factors

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2
Q

What does letter ‘c’ & ‘ab’ stand for in Fc & Fab regions of antibody?

A

Crystallisation

Antibody binding

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3
Q

Name 2 enzymes involved in proteolytic of IgG.

A

Papain & pepsin

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4
Q

Give 6 entities of Ig superfamily.

A
IgG
TCR
Class I MHC
CD4
CD28
ICAM-1
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5
Q

Name the regions contributing to hypervariability of antibody.
Name the most variable part of it.

A

CDR (complement determining regions)

CDR3

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6
Q

Name the structure contributing to flexibility of antibody.

A

Hinge region

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7
Q

Name 2 classes of light chain of antibody.

A

Kappa

Lambda

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8
Q

() stabilises multimeric complexes & transport multimers across epithelial cells.

A

Joining (J) chain

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9
Q

() antibody recognises CDR of another antibody.

A

Anti-idiotypic

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10
Q

Function of IgA.

A

Mucosal immunity

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11
Q

Function of IgD.

A

B cell antigen receptor

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12
Q

Function of IgE.

A

Defense against helminthic parasites

Immediate hypersensitivity

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13
Q

Function of IgG.

A
Opsonisation
Complement activation
ADCC
Neonatal immunity 
Feedback inhibition of B cells
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14
Q

Function of IgM.

A

Naive B cell antigen receptor (monomeric form)

Complement activation

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15
Q

Name the antibody which has the longest and shortest half-life.

A

Longest half-life (IgG, 23 days)

Shortest half-life (IgE, 2 days)

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16
Q

Define hybridoma.

A

Hybrids of normal B cells & myeloma tumour which contain cDNA encoding for monoclonal antibodies.

17
Q

Synthesis, assembly & expression of Ig molecules are regulated by this group of proteins found in endoplasmic reticulum. What is the collective name for this protein & name its 2 entities.

A

Chaperones

Calnexin & Binding protein (BiP)

18
Q

Define class switching.

A

Expression of Ig heavy chain isotopes other than IgM & IgG.

19
Q

Define affinity maturation.

A

Introduction of new amino acid substitution into variable domains of antibody heavy & light chains to create high affinity antibodies.

20
Q

Why does IgG have the longest half-life?

A

IgG is able to bind to neonatal Fc receptor (FcRn) which is also involved for IgG transport from maternal circulation across placental barrier.

21
Q

Which IgG have the longest half-life with most efficient effector functions?

A

IgG1 & IgG2

22
Q

Which IgG has the shortest half-life & why?

A

IgG3 as it binds poorly to FcRn

23
Q

Define affinity.

A

Strength of binding between a single combining site of an antibody & epitope.

24
Q

Define avidity.

A

Overall strength of attachment

25
Q

Name 3 zones involved in immune complex formations.

A

Zone of antigen excess
Zone of equivalence
Zone of antibody excess

26
Q

Name 3 types of antigenic determinant natures.

A
Linear epitopes (denaturation)
Conformational epitopes (denaturation)
Neoantigenic determinant (proteolysis)