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1
Glycoproteins that recognize and bind to a particular antigen with very high specificity
ANTIBODY
2
Made in response to exposure to the antigen
ANTIBODY
3
antibody binding site
PARATOPE
4
at pH 8.6, immunoglobulins appear primarily in the gamma band
ELECTROPHORESIS
5
Antibody belong to a group of serum proteins called .
IMMUNOGLOBULIN
6
the primarily organ where the antigens are destroyed
SPLEEN
7
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
EHRLICH’S SIDE-CHAIN THEORY, SPECIFIC RECEPTOR
8
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 hat antibody with specific fits is made
TEMPLATE THEORY, GENERAL RECEPTOR
9
This now specific antibody enters the circulation, while the antigen remains behind to direct further synthesis or degradation to make more antibodies
TEMPLATE THEORY, GENERAL RECEPTOR
10
Template theory proponent
FELIX HAUROWITZ
11
Most accepted theory for antibody diversity
CLONAL SELECTION
12
Clonal selection theory proponent
NIELS JERNE, MCFARLANE BURNET
13
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 toproliferate
CLONAL SELECTION
14
pre-committed to produce a specific antibody
NAIVE B CELL
15
Immunoglobulin are consists of
4 POLYPEPTIDE CHAIN
16
They worked on immunoglobulin G
GERALD EDELMAN, RODNEY PORTER
17
A flexible Y-shaped molecule with four protein chains
MONOMER
18
2 identical light chains-
KAPPA, LAMBDA
19
it will determine the class of immunoglobulin)
2 IDENTICAL HEAVY CHAIN
20
Stem of monomer and lower parts of Y arms• Responsible for the type and antigen-antibody reaction that occurs
CONSTANT REGION
21
Structure serves as a basis for distinguishing the 5 different classes: IgG, IgA, IgM, IgD and IgE
CONSTANT REGION
22
For complement fixation, skin fixation and placental transfer • No capability to bind the antibody
FRAGMENT CONSTANT REGION
23
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,
VARIABLE DOMAIN
24
H chain IgG
GAMMA
25
H chain IgA
ALPHA
26
H chain
EPSILON
27
H chain IgD
DELTA
28
H chain IgM
MU
29
Refers to the heavy chain that determine the Ig class
ISOTYPE
30
Minor variations of these sequences that are present in some individuals but not others
ALLOTYPE
31
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
32
Possess both constant and variable regions, it is the same for all immunoglobulins
LIGHT CHAIN
33
Kappa: contains of the Ig
65%
34
Lambda: contains of the Ig
35%
35
Ratio of Kappa and Lamba was discovered through
BENCE JONES PROTEIN
36
Connect light chains and light chains
DISULFIDE BOND
37
Found in between CH1 and CH2 • Has high proline and hydrophobic residue • A.K.A. Flexible region
HINGE REGION
38
Causes flexibility in hinge region
PROLINE
39
antigen binding site known also as the paratope
FAB SITE
40
CH2 and CH3, where B cells, T cells and complement bind to
FC REGION
41
mainly done to study the immunoglobulins
FRAGMENTATION OF MONOMER
42
Cleaves the Ig above the hinge region
PAPAIN DIGESTION
43
Cleaves the Ig below the hinge region
PEPSIN DIGESTION
44
Basic Ig structure
MONOMER
45
Secretory component/ piece of IgA/ another class of IgA • Prevents the enzymatic degeneration of enzyme among secretions • With J chain
DIMER
46
J chain is also known as
JOINING CHAIN
47
>2 monomer • IgM- pentamer • 10 valence- 10 binding sites • With J chain
POLYMER
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