Two-Chain Immunoglobulin A Molecules: Abnormal or Normal Intermediates in Synthesis

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Abstract
Immunoglobulin A (γA) myeloma proteins secreted by plasma-cell tumors of mice are of two types, a common four-chain molecule and a rare two-chain (3.9S) molecule. The close similarity between two-chain γA molecules and four-chain γA molecules and their polymers is demonstrated in tryptic peptide maps of isolated polypeptide chains and by precipitin reactions with rabbit antiserums to γA immzunoglobulins. However, a difference between these two types is distinguishable with homologous antiserums. Homologous antiserums to two-chain γA immunoglobulins are specific and do not cross-react with four-chain γA immutnoglobulins.