A low-electrophoretic-mobility H1 histone subfraction from Kirkman-Robbins hamster hepatoma.
A protein showing lower electrophoretic mobility in acidic urea polyacrylamide gels than did the usual histone H1 subfractions has been detected among the H1 histones extracted from chromatin of a transplantable hamster hepatoma, originally induced by Kirkman and Robbins. It was proved to be a true H1 histone subfraction. It differs from the remaining ones by the total chain length, amino acid composition, and isoelectric point value. It is not a phosphorylated or phosphoribosylated metabolic form of another subfraction. Its proteolytic degradation products (obtained by thrombin and trypsin digestion) closely resembled those obtained from other H1 subfractions. The investigated hepatoma seems to provide an interesting model of neoplastic cells showing a distinct difference in histone composition from the homologous normal tissue.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002843:Chromatin / Q000378:metabolism; D002848:Chromatography, DEAE-Cellulose; D006224:Cricetinae; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000032:analysis* / Q000302:isolation & purification; D007526:Isoelectric Point; D008114:Liver Neoplasms, Experimental / Q000378:metabolism; D008970:Molecular Weight; D013917:Thrombin; D014357:Trypsin
D000596:Amino Acids; D002843:Chromatin; D006657:Histones; D014357:Trypsin; D013917:Thrombin