12th Page Flashcards

1
Q

What is the approximate molecular weight of a light chain?

A

~25 kDa

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2
Q

How many amino acids are in a light chain?

A

~220 amino acids

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3
Q

What are the two types of light chains?

A

Kappa (k) and Lambda (λ) chains

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4
Q

Which chromosome is the Kappa light chain located on?

A

Chromosome 2

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5
Q

Which chromosome is the Lambda light chain located on?

A

Chromosome 22

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6
Q

Are both Kappa and Lambda light chains found in all 5 classes of immunoglobulin?

A

Yes, but only one type is present in a given molecule.

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7
Q

What is the approximate molecular weight of a heavy chain?

A

~50 - 70 kDa

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8
Q

How many amino acids are in a heavy chain?

A

~440 amino acids

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9
Q

Which chromosome is the heavy chain located on?

A

Chromosome 14

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10
Q

Ig type in Heavy Chain (GAMED)

A

They are unique to each class and give each Ig type its name: IgG, IgA, IgM, IgE, IgD.

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11
Q

What is the difference between allotype and idiotype?

A

Allotype refers to variations in constant regions (Gm groups), while idiotype refers to variations in variable regions.

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12
Q

Same heavy chain for each class/ H chain that is unique to each antibody

A

Isotype

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13
Q

Hinge region in Heavy chain is located where?

A

It is located between CH1 and CH2.

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14
Q

What is a characteristic finding in the urine of a patient with multiple myeloma?

A

BJP - Bence Jones Proteins

Light chains are found in the urine.

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15
Q

What are the two distinct regions contained in each light and heavy chain?

A

Variable (V) regions and Constant (C) regions.

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16
Q

How many amino acids of the N-terminal in a light chain are in variable region

A

First 110 amino acids

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17
Q

Variable region is also called?

A

Complimentary Determining region

Hypervariable regions

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18
Q

How many constant regions are in a light chain?

A

Single constant region.

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19
Q

How many constant regions are typically found in heavy chains?

A

3 - 4 constant regions.

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20
Q

What forms the basis of antibody classification?

A

Constant regions.

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21
Q

Domains

A

regions in Ab molecule

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22
Q

Components of IgG, IgA, IgD

L-1:1
H-1:3

A

The light chain has 2 domains: 1 VL and 1 CL.

The heavy chain has 4 domains: 1 VH and 3 CH.

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23
Q

What are the components of IgM and IgE?

L-1:1
H-1:4

A

1 light chain (2 domains: 1 VL and 1 CL)

1 heavy chain (5 domains: 1 VH and 4 CH).

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24
Q

Proteolytic/Chemical treatment of immunoglobulins.

A

Pepsin
Papain
Mercaptoethanol

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25
Q

What Ig has monomer structure?

A

Ig GADE

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26
Q

What is the structure of IgA?

A

Monomer and Dimer

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27
Q

What is the structure of IgM?

A

Pentamer

28
Q

What Ig has 75 sedimentation coefficient?

A

Ig GAD

29
Q

What Ig has 195 sedimentation coefficient?

A

IgM

30
Q

What Ig has 85 sedimentation coefficient?

A

IgE

31
Q

What is the molecular weight of IgG?

A

150,000

32
Q

What is the molecular weight of IgA?

A

160,000

33
Q

What is the molecular weight of IgM?

A

900,000

34
Q

What is the molecular weight of IgE?

A

190,000

35
Q

What is the molecular weight of IgD?

A

180,000

36
Q

What is the percent of total immunoglobulin?

IgG

A

70-75

37
Q

What is the percent of total immunoglobulin?

IgA

A

10-15

38
Q

What is the percent of total immunoglobulin?

IgM

A

10

39
Q

What is the percent of total immunoglobulin?

IgD

A

<1

40
Q

What is the percent of total immunoglobulin?

IgE

A

0.002

41
Q

What is the serum half-life of IgG?

A

23 days

42
Q

What is the serum half-life of IgA?

A

5 days

43
Q

What is the serum half-life of IgM?

A

6 days

44
Q

What is the serum half-life of IgD?

A

1-3 days

45
Q

What is the serum half-life of IgE?

A

2-3 days

46
Q

What Ig has C’ fixation?

A

Ig GM

47
Q

What Ig has no C’ fixation?

A

Ig ADE

48
Q

Does Ig only cross the placenta?

A

IgG

49
Q

What are the subclasses of IgG?

A

IgG1, IgG2, IgG3, and IgG4.

They are numbered according to their abundance in the serum: IgG1 > IgG2 > IgG3 > IgG4.

50
Q

Which IgG is the most abundant in blood?

A

IgG

It constitutes approximately 67% of IgG subclasses.

51
Q

Which IgG subclass is most efficient in crossing the placenta?

A

IgG1

IgG2 cannot cross the placenta.

52
Q

Which IgG subclass is most efficient in complement fixation?

A

IgG3

It has the longest hinge region.

53
Q

Which IgG subclass cannot fix complement?

A

IgG4

54
Q

Which IgG subclass cannot cross the placenta?

A

IgG 2

55
Q

IgG3

A

longest hinge region among IgG subclasses

56
Q

Ig of longest half-life

A

IgG

57
Q

Ig with long term immunity

A

IgG

58
Q

Warm antibodies

A

IgG

59
Q

Predominant antibody in secondary

A

IgG

60
Q

Ig of anamnestic immune response

A

IgG

61
Q

Chronic Ig

A

IgG

62
Q

Non-agglutination Ig

A

IgG

63
Q

How many disulfides are there in IgG 1 (67%)

A

2 disulfide bonds.

64
Q

How many disulfides are there in IgG2 (22%)

A

4 disulfide bonds

65
Q

How many disulfides are there in IgG3 (7%)

A

15 disulfide bonds

66
Q

How many disulfides are there in IgG4 (4%)

A

2 disulfide bonds

67
Q

What role do macrophages, monocytes, and neutrophils play regarding IgG?

A

They have receptors on their surfaces that are specific for the FC region of IgG, enhancing contact between antigen and phagocytic cells, and increasing the efficiency of phagocytosis.