ANTIBODIES Flashcards

(84 cards)

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
Constant regions of the H chain are unique to each class and give each immunoglobulin
Constant region (heavy chain)
26
Refers to the heavy chain that determine the Ig class
Isotype
27
Minor variations of these sequences that are present in some individuals but not others
Allotype
28
• 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.
Idiotype
29
Possess both constant and variable regions, it is the same for all immunoglobulins
Light chain
30
Kappa: contains _____ of the Ig Lambda: contains _____ of the Ig
65% 35%
31
How is Lambda and Kappa discovered?
produced by a malignant plasma cell from the urine of Multiple Myeloma patients
32
At what temperature is bence jones proteins gonna precipitate?
60°C
33
Further heating of bence jones at 80 C, the precipitate will _______
Redissolve
34
• Connect heavy chains and heavy chains • Connect heavy chains and light chains • Connect light chains and light chains
Disulfide bond
35
Where is the hinge region found?
CH1 and CH2
36
Hinge region is also known as?
Flexible region
37
What causes the flexibility of the hinge region?
Proline
38
What is the other form of IgA?
Secretory IgA.m
39
In one immunoglobulin, it contains ____ domains
6
40
antigen binding site known also as the paratope
Fab site
41
CH2 and CH3, where B cells, T cells and complement bind to
Fc region
42
• mainly done to study the immunoglobulins • In order to fragment the immunoglobulins, we are going to use enzymes
Fragmentation of monomer
43
Cleaves the Ig above the hinge region
Papain digestion
44
How many fragments of a monomer will Papain digestion give?
3 = 2 Fab and 1 Fc region
45
Cleaves the Ig below the hinge region
Pepsin digestion
46
How many fragments dk pepsin digestion give?
2 = F(ab)2 + Fc
47
This is the basic Ig structure?
Monomer
48
What are the Immunoglobulins that are monomer?
IgG, IgD, IgE, IgA
49
How many binding sites are there in a monomer, dimer and polymer?
M: 2 D: 4 P: 10
50
• 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
Dimer
51
• >2 monomer • IgM- pentamer • 10 valence- 10 binding sites • With J chain
Polymer
52
• Predominant type of immunoglobulin in humans • Longest half-life of any immunoglobulin class o Also known as the secondary antibody in terms of infection
IgG
53
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
Secondary
54
What IgG type is predominant?
IgG1
55
How many disulfide bonds do IgG1, 2, 3, and 4 have?
1 = 2 2 = 4 3 = 15 4 = 2
56
What is the most efficient subclass?
IgG1
57
What are the functions of IgG?
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
Decreased level of IgG can be manifested in?
primary (genetic) or secondary (acquired) Ig deficiencies.
59
Significant increases of IgG are seen in the following conditions:
Infectious diseases Hematologic disorders Collagen disorders
60
expressed as membrane-bound antibody on B cells
Monomeric IgM
61
joining chain, Seen mostly in serum
Pentameric IgM
62
What is the appearance of IgM in free state?
star-like appearance
63
What is the appearance of IgM when combined with Ag?
Crab-like appearance
64
IgM is also known as?
Macroglobulin
65
What immunoglobulin do newborns produce?
IgM
66
Most primitive, first to appear among infants
IgM
67
IgM is Formed in response to stimulus specifically by?
gram-negative bacteria
68
In terms of infections, it will be the first one to increase
IgM
69
If IgM only is present = ___________ If there is no reaction from the IgM and positive for IgG = _________
Acute infection Chronic infection
70
First one to appear in phylogeny and the last to leave in senescence
IgM
71
first test for syphilis), heterophile antibodies, RF (rheumatoid factor), cold agglutinins and allohemagglutinins belong under this type of antibody.
Wasserman test
72
What are the functions of IgM?
Complement fixation Best agglunitin Opsonization Neutralization of toxins
73
10-15% serum immunoglobulin
IgA
74
Monomeric in serum: Occurs as a dimer in secretions:
IgA1 IgA2
75
• Prevents attachment of pathogen to mucosal surface • Prevent enzymatic degradation if IgA • Secretary component will serve as a specific receptor for IgA
Mucosal Immunity
76
responsible for immunoregulation
IgD
77
Where is IgD found?
unstimulated but immunocompetent B cell
78
Postulated as anti-idiotypic antibody involved in a feedback mechanism to switch off B-cells
IgD
79
Where is the location of IgD?
on the surface of a B lymphocyte in association with IgM
80
Least abundant immunoglobulin in the serum
IgE
81
Heat-labile antibodies, originally called as ______________?
Reagin antibody
82
Binds strongly to a receptor on mast cells and basophils and together with antigen, mediates the release of histamine and heparin from these cells
IgE
83
What is the most important function of IgE?
Mediates hypersensitivity reactions, such as allergies, and anaphylaxis, and generally responsible for an individual’s immunity to invading parasites
84
___________ recognizes the IgE attached to parasite to release Major basic protein and Eosinophil Cationic Protein
Eosinophil