What is "immunoglobulin d"

immunoglobulin \im`mu*no*glob"ulin\ ([i^]m`m[-u]*n[-o]*gl[o^]b"[-u]*l[i^]n) n. (1953) any one of a class of globular proteins which are antibodies and are produced by the immune system in animals.

Note: The immunoglobulins form a series of related proteins which are each composed of two pairs of polypeptide chains, called heavy (H) and light (L, meaning of lower molecular weight), all linked together by disulfide bonds. They are subdivided on the basis of the structural and antigenic properties of the H chains into four subgroups, immunoglobulin G (IgG), immunoglobulin A (IgA), immunoglobulin M (IgM), and immunoglobulin D (IgD). They are divided also into subclasses. Both H and L chains of anny given class and subclass have regions which are of constant structure within that class, as well as regions which are of variable structure. The variable regions impart the ability to recognize and bind to specific molecular structures, thus providing the organism the capacity to recognize and defend itself against the harmful effects of substances foreign to the body.
--Stedman

Syn: Ig.

n. one of the five major classes of immunoglobulins; present in blood serum in small amounts [syn: IgD]

Immunoglobulin D (IgD) is an antibody isotype that makes up about 1% of proteins in the plasma membranes of immature B-lymphocytes where it is usually coexpressed with another cell surface antibody called IgM. IgD is also produced in a secreted form that is found in very small amounts in blood serum, representing 0.25% of immunoglobulins in serum. Relative molecular mass and half-life of sIgD is 185 kDa and 2.8 days, respectively. Secreted IgD is produced as a monomeric antibody with two heavy chains of the delta (δ) class, and two Ig light chains.