[Subunit composition and enzymatic properties of myosins from human and rabbit skeletal muscles].
It is shown that myosin of human skeletal muscles is more difficult for purification from the actin and nucleic acids admixtures. It is also characterized by a less yield and a pronounced lability to denaturant effects as compared to rabbit myosin. The ATPase activity of human myosin is 1.5-2 times as low and the cholinesterase one--tens of times as high as those of rabbit myosin. A relative content of LC3 (LC--light chains) is approximately twice as low and that of LC1--as high as in rabbit myosin. It is supposed that the found differences in the properties may be explained to a considerable extent by a different ratio of certain light chains contained in the investigated proteins.
D000251:Adenosine Triphosphatases / Q000032:analysis*; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002802:Cholinesterases / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D006801:Humans; D008970:Molecular Weight; D009132:Muscles / Q000032:analysis* / Q000201:enzymology; D009218:Myosins / Q000032:analysis*; D011817:Rabbits
D002802:Cholinesterases; D000251:Adenosine Triphosphatases; D009218:Myosins; D002118:Calcium
Sostav sub"edinits i fermentativnye svoĭstva miozinov skeletnykh myshts cheloveka i krolika.