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immunoglobulin monomer 375 immunoglobulin μ chain
H2N Ser Cys Cys Gly Gln
Cys
Kappa light chain showing domain structure.
Immunoglobulin light chain.
L chain
Cys
Arg
Photomicrograph of immunoglobulin λ light “staining” by
immunoperoxidase.
H2N Asp Cys Cys Lys Arg
Cys
Cys
Lambda light chain showing domain structure.
also promotes phagocytosis and bacteriolysis through its
complement activation activity.
immunoglobulin monomer
The basic unit of immunoglobulin, comprised of two heavy
chains and two light chains.
immunoglobulin μ chain
A 72-kDa, 570-amino acid heavy polypeptide chain composed
of one variable region designated V H and a constant
region with four domains designated C H1, C H2, C H3, and
C H4. The μ chain does not have a hinge region. A “tail
piece” is located at the carboxyl terminal end of the chain.
It is composed of 18 amino acid residues. A cysteine residue
at the penultimate position of a carboxyl terminal region of
the μ chain forms a disulfide bond that joins to the J chain.
Val
Cys
Cys
Pentameric immunoglobulin M (IgM) consisting of five 7S monomers
composed of two heavy and two light polypeptide chains each and one J
chain per molecule.
Monomeric immunoglobulin M (IgM) that contains two heavy chain
and two κ or two λ light chains.
Photomicrograph of IgM-producing cells (immunoperoxidase staining).
The μ chain of humans has five N-linked oligosaccharides.
Secreted IgM (μ s) and membrane IgM (μ m) and μ chain differ
only in the final 20 amino acid residues at the carboxyl
terminal end. The membrane form of IgM has 41 different
residues substituted for the final 20 residues in the secreted
form. A 26-residue region of this carboxyl terminal section
I