Accessibility of histone H1° and its structural domains to antibody binding in mononucleosomes

FEBS Letters

Zlatanova, Jordanka²  Banchev, Todor¹  Srebreva, Ljuba¹ 

[1] Institute of Molecular Biology, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria;Institute of Genetics, Bulgarian Academy of Sciences, 1113 Sofia, Bulgaria

关键词: Histone H1°;    Structural domain;    Antibody binding;    Mononucleosome;    ELISA;    ELISA;    enzyme-linked immunosorbent assay;    GH5;    globular domain of histone H5;    PMSF;    phenylmethylsulphonyl fluoride;   

DOI  :  10.1016/0014-5793(89)80230-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

This work is devoted to the study of the immunoreactivity of histone H1° and its major structural domains in mononucleosomes. Three types of antibody populations were used: (i) anti-H1° 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 intensifies of the immunoreaction could be interpreted as reflecting the exposure of the antigenic determinants of the individual protein domains in the monosome particle.

【 授权许可】

Unknown