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Identification of a troponin‐I like protein in platelet preparations as histone H2B
Author(s) -
Stewart D.I.H.,
Golosinska K.,
Smillie L.B.
Publication year - 1983
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(83)81130-2
Subject(s) - histone h2b , calmodulin , tropomyosin , troponin c , biochemistry , chemistry , troponin complex , histone , troponin , platelet , atpase , platelet aggregation , microbiology and biotechnology , biology , actin , enzyme , psychology , psychiatry , myocardial infarction , immunology , gene
A tropomyosin‐binding protein (app. M r 17000) was detected in equine platelet preparations by a gel overlay technique. Its isolation, amino acid and partial sequence analyses have shown it to be histone H2B. As with a similar protein from pig platelet preparations [der Terrossian (1983) FEBS Lett. 152, 202–206], it inhibits Mg 2+ ‐dependent actomyosin S1 ATPase. This inhibition is partially reversed in the presence of calmodulin and Ca 2+ but is not potentiated, unlike troponin‐I, by tropomyosin. This protein, along with the other histones, is almost certainly derived from a low level of contaminating nucleated cells in most platelet preparations.