ADP binds similarly to rigor muscle myofibrils and to actomyosin-subfragment one.
The binding of Mg2+ 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.
D000244:Adenosine Diphosphate / Q000378:metabolism*; D000818:Animals; D002417:Cattle; D006352:Heart Ventricles / Q000378:metabolism; D007700:Kinetics; D008274:Magnesium / Q000378:metabolism*; D009119:Muscle Contraction; D009132:Muscles / Q000378:metabolism*; D009206:Myocardium / Q000378:metabolism*; D009210:Myofibrils / Q000378:metabolism*; D015879:Myosin Subfragments; D009218:Myosins / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits; D013696:Temperature
D015879:Myosin Subfragments; D010446:Peptide Fragments; D000244:Adenosine Diphosphate; D009218:Myosins; D008274:Magnesium