Voprosy meditsinskoi khimii (ISSN 0042-8809)

Isolation and properties of myosin from human skeletal muscles

   
Printsev M.D.
PubMed Id: 142366
Year: 1977 vol: 23  issue:3  pages: 291-294
Abstract: 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).
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Reference: Printsev M.D., Isolation and properties of myosin from human skeletal muscles, Voprosy meditsinskoi khimii, 1977, vol: 23(3), 291-294.
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