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ImmunoglobulinG -IgG

ImmunoglobulinG - IgG

Electron microscope studies reveal immunoglobulin G to be a Y-shaped molecule its molecular weight is about 150,000. The enzyme papain cleaves IgG into three active fragments, each of MW 50,000. Two of these fragments bind antigens and are called Fab (F for fragment and a for antigen binding). Each Fab has one antigen binding site. Thus the IgG molecule has two antigen binding sites which bind to antigens and form a precipitate with it .Each IgG molecule binds to two antigen molecules. The overall effect of the action of several IgG molecules is the formation of a lattice.

The third fragment, which forms the lower arm of the Y, is called Fc because it is readily crystallized. It does not bind antigen. Fc can cross placental membrane because it contains a placemental transmission site. In this respect it differs from Fab which cannot cross the membrane. Fe also has a complement binding site.

Each Eab fragment is joined to the Fe fragment by a hinge. The two hinges permit variation in the angle between the two Fab units. Each IgG molecule consists of four polypeptide chains, two identical heavy (H) chains (MW 53,000) and two identical light (L) chains (MW 22,500). This structure is referred to as the L2H2 structure. The heavy chains are at least twice the length of the light chains.

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