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Immunoserology > ANTIBODIES > Flashcards

ANTIBODIES Flashcards

1
Q

Glycoproteins that recognize and bind to a particular antigen
with very high specificity

A

Antibodies

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2
Q

Antigen Binding sites

A

Epitope

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3
Q

(antibody binding site)

A

Paratope

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4
Q

What group of serum proteins does antibodies belong to?

A

Immunoglobulins

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5
Q

Where do immunoglobulins appear primarily?

A

Gamma band

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6
Q

At what band is Albumin found?

A

Alpha bond

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7
Q

At what bond is immunoglobulins found?

A

Gamma band

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8
Q

spleen is the primarily organ where the antigens
are destroyed

A

Reticular Endothelial system

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9
Q

postulated that certain cells had specific surface
receptors for antigen

A

Paul Ehrlich

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10
Q

• Occurred once antigen was introduced, it would select the cell
with proper receptor, combination would take place and
receptors would break off and enter the circulation as
antibody molecules
• New receptors would form in place of those broken off and
enter the circulation as antibody molecules

A

EHRLICH’S SIDE-CHAIN THEORY (SPECIFIC RECEPTOR)

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11
Q

Who postulates the Template theory?

A

Felix Haurowitz

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12
Q

• Antibody producing cells are capable of synthesizing a
generalized type of antibody and when contact with an
antigen occurs, the antigen serves as a mold or template and
alters protein synthesis so that antibody with specific fits is
made
• This now specific antibody enters the circulation, while the
antigen remains behind to direct further synthesis or
degradation to make more antibodies.

A

Template theory

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13
Q

Most accepted theory for antibody diversity. The key premise is that individual lymphocytes are
genetically programmed to produce one type of
immunoglobulin and that a specific antigen finds or selects
those particular cells capable of responding to it, causing it to proliferate.

A

Clonal selection

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14
Q

They independently supported
the idea of clonal selection process for antibody formation.

A

Niels Jerne and Mcfarlane Burnet

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15
Q

Which cell produces the antibody?

A

B-cells

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16
Q

How many polypeptide chains does an antibody contain?

A

4

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17
Q

They worked on Immunoglobulin G (IgG)

A

Gerald Edelman and Rodney Porter

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18
Q

A flexible Y-shaped molecule with four protein chains

A

Monomer

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19
Q

two sections at the end of Y’s arm. Contains also the antigen
binding sites (Fab) or the paratope. The Fab is identical on
the same antibody, but vary from one antibody to another.

A

Variable region

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20
Q

The number of binding sites = _________________?

A

the number of valences

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21
Q

• Stem of monomer and lower parts of Y arms
• Responsible for the type and antigen-antibody reaction that
occurs
• Constant region of heavy chain differs from one antibody
class to the other
• Structure serves as a basis for distinguishing the 5 different
classes: IgG, IgA, IgM, IgD and IgE

A

Constant region

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22
Q

• All of the antibodies have the same Fc region
• Mainly the one attached to the B cells or T cells
• For complement fixation, skin fixation and placental transfer
• No capability to bind the antibody

A

FC (FRAGMENT CONSTANT) REGION

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23
Q

FC region is for?

A

complement fixation, skin fixation and placental transfer

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24
Q

• First approximately 110 amino acids at the amino-terminal
end
• The remaining amino acids can typically be divided up into
two or three or more constant regions with very similar
constant regions with very similar sequences, designated CH1,
CH2, and CH3 (constant heavy chain 1,2,3)

A

Variable domain (heavy chain)

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25
Q

Constant regions of the H chain are unique to each class and
give each immunoglobulin

A

Constant region (heavy chain)

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26
Q

Refers to the heavy chain that determine the Ig class

A

Isotype

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27
Q

Minor variations of these sequences that are present in some individuals but not others

A

Allotype

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28
Q

• The aminoterminal ends of both L and H contain these
regions, which are essential to the formation of the antigen-
binding site
• variable portions of each chain are unique to a specific
antibody molecule.

A

Idiotype

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29
Q

Possess both constant and variable regions, it is the same for
all immunoglobulins

A

Light chain

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30
Q

Kappa: contains _____ of the Ig
Lambda: contains _____ of the Ig

A

65%
35%

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31
Q

How is Lambda and Kappa discovered?

A

produced by a malignant plasma cell from the urine of
Multiple Myeloma patients

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32
Q

At what temperature is bence jones proteins gonna precipitate?

A

60°C

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33
Q

Further heating of bence jones at 80 C, the precipitate will _______

A

Redissolve

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34
Q

• Connect heavy chains and heavy chains
• Connect heavy chains and light chains
• Connect light chains and light chains

A

Disulfide bond

35
Q

Where is the hinge region found?

A

CH1 and CH2

36
Q

Hinge region is also known as?

A

Flexible region

37
Q

What causes the flexibility of the hinge region?

A

Proline

38
Q

What is the other form of IgA?

A

Secretory IgA.m

39
Q

In one immunoglobulin, it contains ____ domains

A

6

40
Q

antigen binding site known also as the paratope

A

Fab site

41
Q

CH2 and CH3, where B cells, T cells and
complement bind to

A

Fc region

42
Q

• mainly done to study the immunoglobulins
• In order to fragment the immunoglobulins, we are going to
use enzymes

A

Fragmentation of monomer

43
Q

Cleaves the Ig above the hinge region

A

Papain digestion

44
Q

How many fragments of a monomer will Papain digestion give?

A

3 = 2 Fab and 1 Fc region

45
Q

Cleaves the Ig below the hinge region

A

Pepsin digestion

46
Q

How many fragments dk pepsin digestion give?

A

2 = F(ab)2 + Fc

47
Q

This is the basic Ig structure?

A

Monomer

48
Q

What are the Immunoglobulins that are monomer?

A

IgG, IgD, IgE, IgA

49
Q

How many binding sites are there in a monomer, dimer and polymer?

A

M: 2
D: 4
P: 10

50
Q

• Secretory component/ piece of IgA/ another class of IgA
• Prevents the enzymatic degeneration of enzyme among
secretions
• With J chain- additional structure, also known as joining
chain

A

Dimer

51
Q

• >2 monomer
• IgM- pentamer
• 10 valence- 10 binding sites
• With J chain

A

Polymer

52
Q

• Predominant type of immunoglobulin in humans
• Longest half-life of any immunoglobulin class
o Also known as the secondary antibody in terms of
infection

A

IgG

53
Q

the next antibody after IgM. It is the one
usually being tested in the laboratory, the presence if
IgG means that there is already a lifelong protection to
a particular disease/ infection

A

Secondary

54
Q

What IgG type is predominant?

A

IgG1

55
Q

How many disulfide bonds do IgG1, 2, 3, and 4 have?

A

1 = 2
2 = 4
3 = 15
4 = 2

56
Q

What is the most efficient subclass?

A

IgG1

57
Q

What are the functions of IgG?

A

Provides immunity to the newborn by crossing through the
placenta
Fixes complement
Opsonization
Neutralization of toxins and viruses
Participation in agglutination and precipitation reaction

58
Q

Decreased level of IgG can be manifested in?

A

primary (genetic)
or secondary (acquired) Ig deficiencies.

59
Q

Significant increases of IgG are seen in the following
conditions:

A

Infectious diseases
Hematologic disorders
Collagen disorders

60
Q

expressed as membrane-bound
antibody on B cells

A

Monomeric IgM

61
Q

joining chain, Seen mostly in serum

A

Pentameric IgM

62
Q

What is the appearance of IgM in free state?

A

star-like appearance

63
Q

What is the appearance of IgM when combined with Ag?

A

Crab-like appearance

64
Q

IgM is also known as?

A

Macroglobulin

65
Q

What immunoglobulin do newborns produce?

A

IgM

66
Q

Most primitive, first to appear among infants

A

IgM

67
Q

IgM is Formed in response to stimulus specifically by?

A

gram-negative bacteria

68
Q

In terms of infections, it will be the first one to increase

A

IgM

69
Q

If IgM only is present = ___________
If there is no reaction from the IgM and positive for
IgG = _________

A

Acute infection
Chronic infection

70
Q

First one to appear in phylogeny and the last to leave in
senescence

A

IgM

71
Q

first test
for syphilis), heterophile antibodies, RF (rheumatoid factor),
cold agglutinins and allohemagglutinins belong under this
type of antibody.

A

Wasserman test

72
Q

What are the functions of IgM?

A

Complement fixation
Best agglunitin
Opsonization
Neutralization of toxins

73
Q

10-15% serum immunoglobulin

A

IgA

74
Q

Monomeric in serum:
Occurs as a dimer in secretions:

A

IgA1
IgA2

75
Q

• Prevents attachment of pathogen to mucosal surface
• Prevent enzymatic degradation if IgA
• Secretary component will serve as a specific receptor for IgA

A

Mucosal Immunity

76
Q

responsible for immunoregulation

A

IgD

77
Q

Where is IgD found?

A

unstimulated but immunocompetent B cell

78
Q

Postulated as anti-idiotypic antibody involved in a feedback mechanism to switch off B-cells

A

IgD

79
Q

Where is the location of IgD?

A

on the surface of a B lymphocyte in association with IgM

80
Q

Least abundant immunoglobulin in the serum

A

IgE

81
Q

Heat-labile antibodies, originally called as ______________?

A

Reagin antibody

82
Q

Binds strongly to a receptor on mast cells and basophils and
together with antigen, mediates the release of histamine and
heparin from these cells

A

IgE

83
Q

What is the most important function of IgE?

A

Mediates hypersensitivity
reactions, such as allergies, and anaphylaxis, and generally
responsible for an individual’s immunity to invading
parasites

84
Q

___________ recognizes the IgE attached to parasite to release
Major basic protein and Eosinophil Cationic Protein

A

Eosinophil

Immunoserology (21 decks)

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