[Muscular myosin structural and functional changes during interaction with ATP and bivalent ions].
The interaction of myosin with ATP and bivalent ions is shown to cause changes in myosin ultraviolet fluorescence. Such a change is more significant for myosin of skeletal muscles than for that of smooth muscles. Kinetics of the fluorescence change has a phase of a sharp rise immediately after ATP addition and a phase of a slow decrease of fluorescence. The changes in fluorescence are connected with formation of an intermediate complex of myosin with ATP (intermediate). It is established that calcium ions are specific in the myosin ATPase reaction and they accelerate considerably the decay of this complex, while magnesium ions inhibits this process.
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D002413:Cations, Divalent; D002417:Cattle; D007700:Kinetics; D009132:Muscles / Q000378:metabolism*; D009218:Myosins / Q000378:metabolism*; D011817:Rabbits; D013050:Spectrometry, Fluorescence
D002413:Cations, Divalent; D000255:Adenosine Triphosphate; D009218:Myosins
Strukturnye i funktsional'nye izmeneniia miozina myshts pri vzaimodeĭstvii s ATP i dvukhvalentnymi ionami.