Primary structure and microheterogeneities of rat chloroleukemia histone H2A (histone ALK, IIbl or F2a2).
Rat chloroleukemia histone H2A, obtained from the F2a2 fraction, has been eluted in two peaks from a Biorex 70 column. The amino acid sequence of rat chloroleukemia histone H2A has been determined and compared to that of calf-thymus histone H2A. The structural studies performed on the tryptic peptides from the maleylated histone and on the thermolysin peptides from the native histone clearly demonstrate the existence of three molecular species of histone H2A depending on the nature of the amino acid residue at positions 16 and 99: H2A-alpha (Ser-16 and Lys-99) accounts for 60% and H2A-betaI (Thr-16 and Arg-99) and H2A-betaII (Ser-16 and Arg-99) for 20% each. A threonine residue at position 16 and a lysine residue at position 99 have been found in calf-thymus histone H2A.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D006657:Histones / Q000302:isolation & purification; D007942:Leukemia, Experimental / Q000032:analysis*; D051381:Rats; D013820:Thermolysin; D014357:Trypsin
D000596:Amino Acids; D006657:Histones; D014357:Trypsin; D013820:Thermolysin