Untitled - D Ank Unlimited

immunoglobulin G (IgG) 371 immunoglobulin λ chain
IgG1 Fab fragment.
immunoglobulin G (IgG)
Immunoglobulin G (IgG) comprises approximately 85% of
the immunoglobulins in adults. It has a molecular weight of
154 kDa based on two light chains of 22,000 Da each and
two heavy chains of 55,000 Da each. It has the longest halflife
(23 days) of the five immunoglobulin classes, crosses
the placenta, and is the principal antibody in the anamnestic
or booster response. IgG shows high avidity or binding
capacity for antigen, fixes complement, stimulates chemotaxis,
and acts as an opsonin to facilitate phagocytosis.
IgG1.
immunoglobulin chain
A 51-kDa, 450-amino acid residue heavy polypeptide chain
comprised of one variable V H domain and a constant region
with three domains designated C H1, C H2, and C H3. The
hinge region is situated between C H1 and C H2. The four
subclasses of IgG in humans have four corresponding γ
chain isotypes, designated γ-1, γ-2, γ-3, and γ-4. IgG 1, IgG 2,
IgG 3, and IgG 4 have differences in their hinge regions and
differ in the number and position of disulfide bonds that
Fab elbow bend
V H
C γ 1
IgG4.
Fab arm waving
C γ 3
IgG2.
IgG3.
C L
C γ 2
V L
Immunoglobulin G (IgG).
Fab rotation
Fc wagging
I