Selective cleavage of skeletal myosin subfragment-1 to form a 26 kDa peptide which shows ATP-sensitive actin binding.
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.
Griffiths
A J
AJ
School of Biochemistry, University of Birmingham, England.
Trayer
I P
IP
D000199:Actins / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D001665:Binding Sites; D008970:Molecular Weight; D015879:Myosin Subfragments; D009218:Myosins / Q000302:isolation & purification / Q000378:metabolism*; D010446:Peptide Fragments / Q000302:isolation & purification / Q000378:metabolism*; D011485:Protein Binding; D013329:Structure-Activity Relationship
D000199:Actins; D015879:Myosin Subfragments; D010446:Peptide Fragments; D000255:Adenosine Triphosphate; D009218:Myosins