[Isolation and properties of myosin from human skeletal muscles].
A method is described for isolation of purified myosin from human sceletal muscles. One isoenzyme of myosin, salting out at 35-45% saturation of ammonium sulfate, was found in aqueous extracts of human muscles. Preparations of myosin, obtained by the method described, possessed the following properties: the ratio of extinctions at 280 and 260 nm 1.5-1.6; the Ca2+-activated ATPase activity--0.15-0.26 mM of phosphorus/mg of protein/min. Molecule of human myosin consisted of two heavy and two light chains (by polyacrylamide gel electrophoresis).
D000251:Adenosine Triphosphatases / Q000032:analysis; D000328:Adult; D002118:Calcium; D006801:Humans; D007527:Isoenzymes / Q000032:analysis; D008875:Middle Aged; D009132:Muscles / Q000032:analysis* / Q000201:enzymology; D009218:Myosins / Q000032:analysis / Q000302:isolation & purification
D007527:Isoenzymes; D000251:Adenosine Triphosphatases; D009218:Myosins; D002118:Calcium
Vydelenie i svoĭstva miozina skeletnoĭ muskulatury cheloveka.