Identification of a troponin‐I like protein in platelet preparations as histone H2B

FEBS Letters

Stewart, D.I.H.¹  Golosinska, K.¹  Smillie, L.B.¹ 

[1] Medical Research Council Group in Protein Structure and Function, Department of Biochemistry, University of Alberta, Edmonton T6G 2H7, Canada

关键词: Tropomyosin binding;    Calmodulin;    Actin binding;    Actomyosin ATPase;    Ca2+ regulation;    SDS;    sodium dodecyl sulfate;    EGTA;    ethylene glycolbis(β-amino-ethyl ether)-N;    N;    N′;    N′-tetraacetic acid;    TM;    tropomyosin;    Tn-T;    troponin-T;    Tn-I;    troponin-I;    Tn-C;    troponin-C;    kDa;    kilo dalton;    DTT;    dithiothreitol;   

DOI  :  10.1016/0014-5793(83)81130-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 Mg²⁺-dependent actomyosin S1 ATPase. This inhibition is partially reversed in the presence of calmodulin and Ca²⁺ 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.

【 授权许可】

Unknown