Selective cleavage of skeletal myosin subfragment‐1 to form a 26 kDa peptide which shows ATP‐sensitive actin binding

FEBS Letters

Griffiths, A.Jane¹  Trayer, Ian P.¹ 

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

关键词: Myosin;    Muscle contraction;    ATP binding;    Protein fragmentation;    S1;    myosin subfragment 1;    S1(A1) and S1(A2);    rabbit fast twitch muscle myosin subfragment 1;    prepared by chymotryptic digestion and containing either the alkali 1 (A1 or LC1) light chain or the alkali 2 (A2 or LC3) light chain;    SDS-PAGE;    polyacrylamide gel electrophoresis in the presence of 0.1% SDS;   

DOI  :  10.1016/0014-5793(89)80484-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A 26 kDa peptide has been cleaved from the C-terminus of the S1 heavy chain with formic acid. Cleavage occurs in the ‘50 kDa’ domain probably at the Asp-600-Pro-601 bond. This fragment has been renatured in the presence of the A2 light chain and the 26 kDa(A2) complex shown to interact with actin in an ATP-sensitive manner.

【 授权许可】

Unknown