期刊论文详细信息
FEBS Letters | |
Selective cleavage of skeletal myosin subfragment‐1 to form a 26 kDa peptide which shows ATP‐sensitive actin binding | |
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
【 预 览 】
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RO201912020291453ZK.pdf | 628KB | download |