부산대학교 도서관

The variants of the core histones of Pisum sativum L. cv. Lincoln have been resolved by two-dimensional polyacrylamide gel electrophoresis. Acetic acid, 8 M urea, 7.2 mM Triton X-100 was used in the first dimension. The second dimension was run in the presence of either anionic (sodium dodecylsulphate) or cationic (cetyltrimethyl-ammonium bromide) detergents. Four putative variants were found for the H2A histone class, 4 for H3 and 3 for H2B. Peptide mapping with Staphylococcus aureus V8 protease was used, together with other criteria, to characterize the variants. The pattern of histone variants is not organ-specific and, in an attempt to determine whether the diversity of histone variants plays some functional role, the kinetics of release of core histones by extensive DNase I digestion of nuclei was studied. H2A and H2B were released under our conditions of digestion, but the time course of release of the different H2A variants showed a certain specificity. [ABSTRACT FROM AUTHOR]