Accessibility of histone H1(0) and its structural domains to antibody binding in mononucleosomes.
This work is devoted to the study of the immunoreactivity of histone H1(0) and its major structural domains in mononucleosomes. Three types of antibody populations were used: (i) anti-H1(0) which reacted with antigenic determinants situated along the whole polypeptide chain; (ii) anti-GH5 which recognized epitopes located in the globular region; and (iii) anti-C-tail antibodies reacting specifically with fragment 99-193 of the protein molecule. The anti-GH5 antibodies gave a weak reaction, the C-tail-specific antibodies reacted relatively strongly and the antiserum to the intact molecule showed an intermediate level of reactivity. The relative intensities of the immunoreaction could be interpreted as reflecting the exposure of the antigenic determinants of the individual protein domains in the monosome particle.
Banchev
T
T
Institute of Molecular Biology, Bulgarian Academy of Sciences, Sofia.
Srebreva
L
L
Zlatanova
J
J
D000818:Animals; D000906:Antibodies / Q000276:immunology*; D000918:Antibody Specificity; D000941:Antigens / Q000276:immunology; D004797:Enzyme-Linked Immunosorbent Assay; D000939:Epitopes / Q000276:immunology*; D006657:Histones / Q000276:immunology* / Q000378:metabolism; D015151:Immunoblotting; D008099:Liver / Q000648:ultrastructure*; D051379:Mice; D009707:Nucleosomes / Q000378:metabolism*; D009994:Osmolar Concentration; D010446:Peptide Fragments / Q000276:immunology; D012965:Sodium Chloride / Q000494:pharmacology
D000906:Antibodies; D000941:Antigens; D000939:Epitopes; D006657:Histones; D009707:Nucleosomes; D010446:Peptide Fragments; D012965:Sodium Chloride