The G4 Subclass in IgG Fractions Prepared by Ion-Exchange Chromatography

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Abstract
Human immunoglobulin IgG consists of four distinct groups of molecules, known as the subclasses of IgG and referred to as G1, G2, G3 and G4 (1–3). Antigenic and structural differences between the four subclasses are located on the heavy chains of the molecules (4, 5). Molecules of both light chain types, κ and λ, are represented in all IgG subclasses. All four subclasses can be demonstrated in normal human serum by immunodiffusion tests with subclass-specific antisera. So far, techniques for the isolation of IgG subclasses from normal human serum have not been developed. This communication reports qualitative differences in the subclass composition of IgG purified by some of the most common chromatographic methods. Antisera were prepared in Rhesus monkeys1 by immunization with isolated IgG myeloma proteins of the different subclasses and made monospecific by appropriate absorption. When tested in Ouchterlony analysis and immunoelectrophoresis, the specific antisera reacted with isolated myeloma proteins of both light chain types of the respective subclass.

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