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  • Title: [Electrophoretic study of the acid soluble proteins of Saccharomyces cerevisiae yeast chromatin].
    Author: Suchilene SP, Gineĭtis AA.
    Journal: Mol Biol (Mosk); 1978; 12(4):863-7. PubMed ID: 355866.
    Abstract:
    Fractionation of acid-soluble proteins from yeast Saccharomyces cerevisiae chromatin by gel electrophoresis suggested the existence of four histonestone fractions--H2a, H2b, H3, H4 and histone H1-like protein. The latter was isolated according to the second method of Johns and extracted with 5% HClO4. Amino acid analysis of the histone H1-like protein showed a moderately high content of basic amino acids, but a much lower ratio of lysine: arginine (approximately 3) than that of the hisone H1 from higher eukaryotes. In addition to histone H1-like protein a protein X was also extracted with 5% HC1O4. The sequence of the electrophoretic mobilities of histone fractions from yeast coincides with those of histone fractions from plants--H4 greater than H3 greater than H2a greater than H2b greater than H1.
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