Immunoglobulin Structure and Function Flashcards

1
Q

what are two forms of antibodies

A

membrane bound

Secreted

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2
Q

antibodies are found on the surface of what cell and function as what

A

B - cells

B-cell receptors

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3
Q

Secrete antibodies bind what

A

antigens

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4
Q

what are 3 functions of secreted antibodies

A

neutralize toxins
prevent entry and spread of pathogen
eliminate microbes

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5
Q

Proteolytic cleavage of antibodies by papain creates what structures

A

Fc - determines function

Fab - determines recognition, 2 separate pieces

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6
Q

what is labelling on Fab fragment

A

single antigenic binding region

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7
Q

Proteolytic cleavage by pepsin creates what structures

A

F(ab’)2

pFc’ (one piece)

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8
Q

what makes antibodies flexable

A

hinge region

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9
Q

what is the role of the constant region of the antibody

A

imparts function of antibody to molecule

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10
Q

is there genetic variation in constant region

A

little

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11
Q

affinity

A

strength of binding b/w single Ab arm and Ag epitope

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12
Q

affinity is expressed how

A

dissociation constant (Kd)

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13
Q

avidity

A

overall strength of attachment of Ab and antigen

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14
Q

Immunoglobin molecule consists of what

A

2 identical heavy chains

2 identical light chains

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15
Q

Domain

A

in both H and L

110 amino acid residues

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16
Q

Light chain consists of what two domains

A

constant (C) domain

variable (V) domain

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17
Q

What region is located on the variable domain of the light chain

A

complementarity determining regions (CDR)

hypervariable region

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18
Q

What domains does Heavy chain have

A

variable domain

several constant domains

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19
Q

within the variable domain the heavy chain has what

A

3 CDRs or hypervariable regions

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20
Q

antigen binding occurs with what domains

A

Variable heavy

variable light

21
Q

how do the CDR regions of antibody form antigen combining site

A

folding of Heavy and Light chains

22
Q

Where is hinge region found

A

Heavy chain

23
Q

isotypes

A

5 types of immunoglobulins (antibody) based off of Heavy chain constant regoin

24
Q

what are the 2 types of Light chains based on their constant region

A

kappa

lambda

25
Q

Is there a difference in function for kappa and lambda

A

no

26
Q

within a single immnoglobulin molecule how many types of light chains are present

A

one

either 2 kappa or 2 lambda

27
Q

do the isotopes have different chemical properties like molecular weight and half life?

A

yes

28
Q

what are 4 functions of isotypes

A

receptor
neutralize/block activity
Ag-Ab complex recognition via Fc receptors
serum complement activation

29
Q

agglutination of isotypes

A

process of neutralization can occur in solution or on surface of cell

30
Q

the process of agglutination does what to the cell

A

phagocytized or removed from circulation

31
Q

opsonization of isotypes?

A

coating surface with antibody

32
Q

the classical pathway for complement uses what for starting point

A

antibody

33
Q

phagocytosis or removal of antibody bound material happens through what

A

receptor mediated event on the phagocyte (FcR)

34
Q

special function of IgA

A

cross mucosal epithelial membrane via Poly Ig receptor

35
Q

special function of IgE

A

coat mast cells allowing release of their granules upon allergen binding

36
Q

special function of IgG

A

sensitize NK cells and eosinophils via FCR

37
Q

which immunoglobin has the highest concentration of serum of normal individuals

A

IgG

38
Q

what are the polymeric antibodies

A

IgM

IgA

39
Q

how are polymeric antibodies stablized

A

J chain

40
Q

in antibody maturation, IgM changes to

A

IgG

41
Q

In order for IgM to change to IgG what must happen in recognition of antigen

A

recognition of same antigen from primary to secondary response

42
Q

what defines an isotype

A

epitopes on constant region

no variation by member of same species

43
Q

Allotype defined by

A

epitopes on constant region

show variation by members of same species

44
Q

idiotype

A

epitopes on variable region

show variation within same individual

45
Q

xeogeneic

A

non human

46
Q

chimeric

A

66% human

47
Q

humanized

A

90-95% human

48
Q

fully humanized

A

human