Molecular homogeneity of the histone content of HeLa chromatin subunits.
Interaction of affinity chromatographically purified antihistone H3 and antihistone H4 with isolated HeLa core particles, followed by separation of unreacted and reacted particles by sedimentation, demonstrates that every core particle contains these histones. Taken together with our previous data indicating the presence of H2B in every nucleosome (Simpson, R. T., and Bustin, M. (1976), Biochemistry 15, 4305), these data lead to the conclusion that each core particle contains two each of the four smaller histones. In contrast to the lack of interference in binding of more than one molecule of antibody to a single species of histone to the core particle, steric hindrance exists when attempts are made to bind both anti-H3 and anti-H4 to core particles.
D000906:Antibodies; D001666:Binding Sites, Antibody; D002843:Chromatin / Q000032:analysis* / Q000648:ultrastructure; D003168:Complement Fixation Tests; D004306:Dose-Response Relationship, Immunologic; D006367:HeLa Cells / Q000032:analysis; D006657:Histones / Q000032:analysis* / Q000276:immunology; D008970:Molecular Weight
D000906:Antibodies; D002843:Chromatin; D006657:Histones