Premium
Accessibility of histone H1° and its structural domains to antibody binding in mononucleosomes
Author(s) -
Banchev Todor,
Srebreva Ljuba,
Zlatanova Jordanka
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80230-3
Subject(s) - histone h1 , histone , microbiology and biotechnology , chemistry , computational biology , biophysics , biology , biochemistry , dna
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.