Proteolytic digestion studies of chromatin core-histone structure. Identification of limit peptides from histone H2B.
Trypsin digestion of chicken erythrocyte chromatin results in a well-defined set of limit peptides derived from the core histones (P1-P5). Two peptides running in sodium dodecyl sulphate gel electrophoresis at the positions of P2 and P3 have been identified as histone H2B residues 21-125 and 24-125. No C-terminal residues are therefore lost from histone H2B. The N-terminal sequence removed correlates well with that having low sequence conservation and not with that showing the greatest basicity. The same correlation was reported previously by us for histone H2A.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002645:Chickens; D002843:Chromatin / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000032:analysis*; D006657:Histones / Q000032:analysis*; D010446:Peptide Fragments / Q000302:isolation & purification*; D014357:Trypsin
D000596:Amino Acids; D002843:Chromatin; D006657:Histones; D010446:Peptide Fragments; D014357:Trypsin