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Selective cleavage of skeletal myosin subfragment‐1 to form a 26 kDa peptide which shows ATP‐sensitive actin binding
Author(s) -
Griffiths A.Jane,
Trayer Ian P.
Publication year - 1989
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(89)80484-3
Subject(s) - myosin , cleavage (geology) , actin , peptide , actina , chemistry , biophysics , biochemistry , biology , cytoskeleton , paleontology , fracture (geology) , cell
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.