Differential binding of rabbit fast muscle myosin light chain isoenzymes to regulated actin

FEBS Letters

Trayer, Hylary R.¹  Trayer, Ian P.¹ 

[1] Department of Biochemistry, University of Birmingham, PO Box 363, Birmingham B15 2TT, England

关键词: Actin binding;    Myosin subfragment 1 isoenzyme;    Regulated actin;    Cooperative binding;    S1;    myosin sub fragment 1;    S1(A1);    S1(A2);    rabbit fast-twitch muscle myosin subfragment 1 containing either the alkali 1 (A1 or LC1) light chain or the alkali 2 (A2 or LC2) light chain;    AdoPP[NH]P;    adenosine-5' -[β;    gg-imido]triphosphate;    Ap5A;    P 1;    P 5;    P1P5-di(adenosine-5')pentaphosphate;    Tn-I;    troponin I;    the inhibitory component of troponin;   

DOI  :  10.1016/0014-5793(85)81065-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The direct binding of S1(A1) and S1(A2) to regulated actin has been investigated by centrifugation. Binding was measured in the presence of either Mg·AdoPP[NH]P or Mg·ADP at 24°C at various ionic strengths. At low ionic strength, in either the presence or absence of Ca²⁺, the binding of S1(A1) to regulated actin was always stronger than for S1(A2). As the ionic strength was increased the differential binding between S1(A1) and S1(A2) was still maintained in the presence of Ca²⁺ but not in its absence. These data are discussed in terms of a modifying role for the N-terminal region of the A1 light chain in regulation of the contractile process.

【 授权许可】

Unknown