ANTIBODY Flashcards

1
Q

humoral immunity is based on the secretion of production of what component?

A

anti bodies

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2
Q

The fully differentiated type of lymphocyte that is The main objective of the ____is to
release or secrete antibodies

A

plasma cells

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2
Q

t cell or b cell?

humoral immunity

A

b cell

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3
Q

Cluster differentiation or surface marker
that remain on the cell surface throughout
the subsequent developmental stages of the B CELL:

A

CD19, CD24, and CD45R

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4
Q

____ is the surface protein that is found on
both activated cells and B cells and act as a
receptor for IL-2

A

CD25

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5
Q

antibodies are also known as the

A

Immunoglobulins

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6
Q

what cytokine is responsible and acting as a receptor for the surface protein that is found on both activated cells and b cells

A

interleukin 2

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7
Q

Glycoprotein found in the serum portion of the
blood.

A

immunoglobulins

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8
Q

where can we found the antibodies?

A

serum portion of the blood

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9
Q

what is the composition of the immunoglobulins.

give the percentage each composition

A

82-96%→polypeptides (protein)
2-14%→carbohydrates

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10
Q

HWO CAN WE BE ABLE TO DISTINGUISH THE BEHAVIOR OF THE IMMUNOGLOBULINS?

A

THROUGH ELECTROPHORESIS

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11
Q

materials of substances we can use for electrophoresis that is based on pH

A

cellulose acetate and citrate agar

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12
Q

what is the pH level of cellulose acetate we used for electrophoresis

A

alkaline - 8.6

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13
Q

what should be the pH level if we will use the citrate agar for electrophoresis

A

6 - 6.3 - acidic

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14
Q

In what region we can found the immunoglobulins?

A

gamma region (y)

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15
Q

since we can found the immunoglobulins in gamma region, we can call it as well as

A

gamma globulins

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16
Q

technically, what is the pH level we need for electrophoresis?

A

8.6

(transes based - we use agarose gel if 8.6 pH is needed)

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17
Q

immunoglobulins plays an essential role
what are the functions:

A

antigen recognition
immune response
capable during opsonization
complement activation

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18
Q

what are the classification of the immunoglobulins

A

GAMDE
IgG
IgA
IgM
IgD
IgE

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19
Q

___is the most abundant protein when it comes
to the serum electrophoresis

A

Albumin

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20
Q

Immunoglubulin is designated as ___

A

Ig

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21
Q

what is the arrangement of the protein or region in the serum electrophoresis

start from albumin to gamma region

A

albumin
alpha 1 globulins
alpha 2 globulins
beta globulins
gamma region

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22
Q

the arrangement of the regions/proteins in the serum electrophoresis is based on ___

A

net charge

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23
Q

what are the proteins under alpha 1 globulins

A

Alpha-1 Antitrypsin (AAT)
Alpha Fetoprotein (AFP)

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24
Q

what are the proteins under alpha 2 globulins

A

ceruloplasmin
haptoglobin,
alpha-2 macroglobulin

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25
Q

what are the proteins under beta globulins

A

transferrin
hemopexin,
complement system
fibrinogen
lipoprotein (LDL, HDL, VLDL)

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26
Q

There is a possibility of an abnormal pattern in serum
electrophoretic activity called the ___, which is in line with the beta
region

A

Beta–gamma bridging (curved)

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27
Q

it can be used as a screening test for certain clinical disease

A

electrophoresis

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28
Q

what disease is associated with an abnormal pattern in line with the Beta region

A

liver cirrhosis

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29
Q

The spike pattern within the gamma region is associated with ___

A

multiple myeloma (elevated plasma
protein)

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30
Q

which immunoglobulin is elevated for patients with multiple myeloma

A

IgG immunoglobulin gamma

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31
Q

Common/significat protein found in URINE with MULTIPLE MYELOMA is called

A

Bence-Jones proteins

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32
Q

Bence-Jones proteins are mainly associated with which chain of the antibodies

A

Light chain

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33
Q

The Bence-Jones proteins are distinguished by
precipitating for about____ and will dissolve at
___.

A

60 Celsius; 80 Celsius

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34
Q

what will happen to a bence-jones protein in 60 degree celsius?

A

it will precipitate

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35
Q

what will happen to a bence-jones protein in 80 degree celsius?

A

it will be dissolve

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36
Q

All immunoglobulin molecules are made up how many basic chain of polypeptide nit?

A

4 basic chain

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37
Q

4 basic chain of polypeptide unit for immunoglobulin is made up of how many heavy and light chain?

A

2 large heavy chain
2 small light chain

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38
Q

The chains of immunoglobulin are held together by noncovalent forces
called the ____

A

disulfide linkage/bond

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39
Q

The four chain polypeptides can be connected
through ___

A

disulfide linkage/bond

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40
Q

Structure of Immunoglobulins was first describe by two scientists.

who are they?

A

Gerald Edelman and Rodney Porter

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41
Q

disulfide linkage/bond is also called as

A

disulfide interchain bridges

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42
Q

which immunoglobulin do Gerald Edelman and Rodney Porter studied?

A

Ig G - immunoglobulin gamma

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43
Q

after ultra centrifugation of Ig G- they were able to find the ___

A

sedimentation coefficient value

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44
Q

what is the sedimentation coefficient value of IgG

A

7s (Svedberg unit)

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45
Q

___ indicates the sedimentation rate in an analytical
ultracentrifuge

A

Svedberg unit

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46
Q

before they used the analytical ultracentrifugation, they need to ___ the Ig G

A

purify

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47
Q

On obtaining a purified preparation of
IgG. Edelman used ___to unfold the molecule.

A

7M (7 Molar Urea)

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48
Q

reagent used in order to unfold the Ig G molecule

A

7M (Molar Urea)

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49
Q

Once the Ig G molecule is unfolded, the exposed sulfhydryl bonds could be cleaved by a reducing agent such as ____

A

2-Mercapthoethanol

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50
Q

2-Mercapthoethanol will reduce the exposed bonds which is the

A

bonds

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51
Q

after the second ultracentrifugation, we will be able to come up to a sediment coefficient of ___

A

3.5 S and 2.2 S

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52
Q

3.5 S fraction has a molecular weight of approximately ___ Da.

A

50,000

53
Q

2.2 S fraction has a molecular weight of
approximately ____Da

A

22,000

54
Q

3.5 S fraction is designated to which chain?

A

heavy chain.

55
Q

2.2 S fraction is designated to which chain?

A

Light chain

56
Q

Gerald Edelman and Rodney Porter won the novel
prize in ___in ____
They were the first ones to describe the structures
of immunoglobulins.

A

1972 ; Physiology and Medicine Practice.

57
Q

This is used to determine the structure of the immunoglobulin

A

ANALYTIC ULTRACENTRIFUGE

58
Q

What are the regions of immunoglobulins

A

Fab and Fc region

59
Q

FAB region - FAB means

A

Fragment antigen binding

60
Q

FC region - FC means

A

Fragment crystallizable

61
Q

who introduced papain digestion?

A

Rodney Porter

62
Q

Papain digestion is Cleaves antibody into three fragments, what are those?

A

2 Fab
1 Fc

63
Q

a type of fragment that has
no antigen binding ability. It is now known to
represent the carboxy terminal halves of Two heavy chains that are held together by SS bonding

A

Fragment crystallizable (Fc region)

64
Q

a fragment that is mainly associated with the
antigen binding

A

Fab region - fragment antigen binding region

65
Q

what are the fragments found in pepsin digestion

A

1fab and 1 fc

66
Q

immunoglobulins that has
2 domain in light chain
4 domain in heavy chain

A

GAD -
IgG
IgA
IgD

67
Q

immunoglobulins that has
2 domain in light chain
5 domain in heavy chain

A

EM -
IgE
IgM

68
Q

Each Fab Fragment of Papain has how many chains

A

1 L chain and ½ of H
chain

69
Q

Each FC Fragment of Papain has how many chains

A

two halves of H chain

70
Q

Each FAB Fragment of pepsin has how many chains

A

2 L chain and two halves of H
chain

71
Q

Each FC Fragment of pepsin has how many chains

A

two halves of H chain

72
Q

The structure of light chains is not fully discovered
until the discovery of an abnormal protein produces
by patients with ____.

A

multiple myeloma

73
Q

Analysis of several Bence-Jones proteins revealed
that there were two main types of L chains.

what are those?

A

kappa and lambda

74
Q

type of light chain

Kappa is designated in what chromosome?

A

chromosome 2

75
Q

type of light chain

lambda is designated in what chromosome?

A

chromosome 22

76
Q

amino acid of kappa

A

200

77
Q

amino acids of lambda

A

220

78
Q

The FC regions of pepsin is ___

A

disintegrated into smaller pieces

79
Q

the fragment associated with the variable region

A

FAB

80
Q

the fragment associated with constant region

A

FC

81
Q

variable regions associated with the FAB is located in the

A

amino terminal end

82
Q

constant regions associated with the FC is located in the

A

carboxyl terminal end

83
Q

a chain that detects the immunoglobulin class

A

heavy chain

84
Q

Constant regions of the H chain are unique to each
class and give each immunoglobulin type its name.

IgG has a/an -__
IgM has a/an __
IgE has a/an - __
IgD has a/an - ___
IgA has a/an - __

A

IgG has a/an - Gamma chain “ɣ”
IgM has a/an - Mu chain “μ”
IgE has a/an - Epsilon chain “ɛ”
IgD has a/an - Delta chain “ẟ”
IgA has a/an - Alpha chain “α”

85
Q

what are the ANTIBODY VARIATION

A

isotype
allotype
idiotype

86
Q

the identity of immunoglobins are the same but they have unique characteristics given by what region

A

variable region - as they have the capacity during the antigen binding

87
Q

a region associated on how they attached to a particular antigen - will provide unique characteristics as well to the antibody

A

variable region

88
Q

antibody variation that has

unique amino acid sequence that is
COMMON to ALL immunoglobulin molecules of a given
class in a given species

A

Isotype

89
Q

antibody variation that has

MINOR VARIATION of these sequences, some immunoglobulins are present but not with the others

A

Allotype

90
Q

In allotype, it is based on what region of an immunoglobulin

A

constant region

91
Q

antibody variation that has subclasses

A

Allotype

92
Q

immunoglobulins that belongs in allotype variation

A

IgG and IgA

IgG has four subclasses and IgA
has two subclasses

93
Q

a type of light chain that is an example of allotype

A

kappa chain

94
Q

antibody variation that has

– variations in the variable region

A

Idiotype

95
Q

Constant region is designated as ___ in Heavy chain

A

CH1, CH2, CH3

96
Q

The segment of Heavy chain located between the CH1
and CH2 regions is known as the ___

A

hinge region

97
Q

In heavy chain, the hinge region is can be found between what regions?

A

ch1 and ch2

98
Q

amino acids for hinge region is the

A

proline

99
Q

the amino acids, proline, for heavy chains allows___

A

it allows for FLEXIBILITY that makes the
ANTIGEN BINDING SITES WORK INDEPENDENTLY

100
Q

immunoglobulins that has hinge region

A

IgG, IgD, IgA

101
Q

immunoglobulins that has NO hinge region

A

IgE, IgM

102
Q

a particular factor which we can determine the antigen binding site if an immunoglobulin

A

valence

103
Q

what are the basic immunoglobulin structures?

A

monomer
dimer
polymer

104
Q

how many binding sites do monomer has?

A

2 binding sites

105
Q

how many binding sites do dimer has

A

4 binding sites

106
Q

how many binding sites do polymer has

A

more than 4

107
Q

an example of monomer

A

IgM (surface area of B cells),
IgE
IgG
serum IgA
IgD

108
Q

an example of dimer

A

Secretory IgA

109
Q

an example of polymer

A

IgM – has 10 valence

110
Q

how many valence do IgM has?

A

10 valence - 10 binding sites - 5 sungay

111
Q

an immunoglobulin that has 23 days half life

A

IgG

112
Q

___is the most predominant immunoglobulin in
humans

A

IgG

113
Q

IgG constitutes how many percent of the total serum immunoglobulins

A

70% to 80%

114
Q

the mnemonic ____

(from most
predominant
to LEAST)

A

GAMDE

115
Q

IgG is best at what reaction due to it’s relatively small size, this reaction is better than agglutination

A

precipitation reaction

116
Q

There are four major subclasses of IgG

A

IgG1, 67%;
IgG2, 22%;
IgG3, 7%;
IgG4, 4 %

117
Q

The subclasses of IgG differ mainly in the number and position of the disulfide bridges between the γ
chains. (in conjunction with heavy-to-heavy chains)

give the corresponding disulfide bonds of each subclasses

A

 IgG1 – two disulfide bonds
 IgG2 – four disulfide bonds
 IgG3 – five disulfide bonds; has the largest hinge region
 IgG4 – two disulfide bonds

118
Q

which IgG subclass has the largest and the most number of disulfide bonding and hinge region?

A

IgG3

119
Q

Which immunoglobulin can cross placenta?

A

IgG

120
Q

which subclasses of IgG can cross planceta?

A

all IgG can cross except for IgG2

121
Q

which subclasses of IgG is the most efficient one for crossing placenta?

A

IgG1

122
Q

can IgG helps in complement fixation?

A

yes, but the IgM is the special one for that

123
Q

which subclass of IgG can’t help with complement fixation?

A

IgG4

124
Q

can IgG react with agglutination reaction?

A

Yes, but not efficiently as they are small

125
Q

what are the characteristic of IgG

A

precipitation reaction
little complement fixation
Opsonization
Neutralization of toxins and viruses
Participation during agglutination (with enhancement medium)

126
Q

which serologic reaction do IgG is the best?

A

precipitation reaction

127
Q

a reaction in which the soluble antigen reacts to the small antibody

A

precipitation reaction

128
Q

an immunoglobulin that needs an enhancement region to perform with agglutination reaction

A

IgG

129
Q
A