[Electrophoretic study of the acid soluble proteins of Saccharomyces cerevisiae yeast chromatin].
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.
D002843:Chromatin / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D005656:Fungal Proteins / Q000302:isolation & purification*; D006657:Histones / Q000302:isolation & purification*; D012441:Saccharomyces cerevisiae / Q000648:ultrastructure*
D002843:Chromatin; D005656:Fungal Proteins; D006657:Histones
Elektroforeticheskoe issledovanie kislotorastvorimykh belkov khromatina drozhzheĭ Saccharomyces cerevisiae.