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ADP binds similarly to rigor muscle myofibrils and to actomyosin‐subfragment one
Author(s) -
Johnson Robert E.,
Adams Patricia H.
Publication year - 1984
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(84)81067-4
Subject(s) - myofibril , myosin , biophysics , chemistry , actina , skeletal muscle , biochemistry , biology , anatomy , cytoskeleton , cell
The binding of Mg 2+ ADP to both rabbit skeletal and bovine cardiac myofibrils has been studied at two different temperatures. In each case a single class of binding sites was observed with a binding constant very close to that reported for the analogous actomyosin‐subfragment one but much weaker than that seen with the analogous myosin subfragment one alone. These findings are discussed in terms of the constraints on the myosin cross‐bridges imposed by the regular array of thick and thin filaments found in myofibrils.