Biochemical and immunological characterization of two distinct variants of histone H2A in Friend leukemia

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Abstract
Changes in the relative amount of 2 histone H2A subfractions were observed in cells at different proliferative stages of Friend mouse leukemia. Biochemical analyses of purified H2A subfractions revealed differences in primary structure, and not the result of postsynthetic modifications of the same parent protein. Antibodies raised against purified H2A.2 subfraction cross reacted with H2A.1 and H2A.2, but showed high specificity for the immunizing subfraction at higher sera dilutions. Only H2A.2 contains a methionine which appears critical to an antigenic difference that immunologically distinguishes H2A.2 from H2A.1. The observed change in the relative amounts of 2 nonallelic variants of a histone coincident with changes in the physiologic states of the cell may indicate a correlation between genome structure and function.

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