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- W1497478067 abstract "A myosin-like protein was purified from amoebae of the cellular slime mold Dictyostelium discoideum. The purification utilized newly discovered solubility properties of actomyosin in sucrose. The amoebae were extracted with a 30% sucrose solution containing 0.1 m-KCl, and actomyosin was selectively precipitated from this crude extract by removal of the sucrose. The myosin and actin were then solubilized in a buffer containing KI and separated by gel filtration. The purified Dictyostelium myosin bears a very close resemblance to muscle myosin. The amoeba protein contains two heavy chains, about 210,000 molecular weight each, and two classes of light chains, 16,000 and 18,000 molecular weight. Dictyostelium myosin is insoluble at low ionic strength and forms bipolar thick filaments. The myosin possesses ATPase activity that is activated by Ca2+ but not EDTA, and is inhibited by Mg2+; under optimal conditions the specific activity of the enzyme is 0.09 μmol P1/min per mg myosin. Dictyostelium myosin interacts with Dictyostelium actin or muscle actin, as shown by electron microscopy and by measurements of enzymatic activity. The ATPase activity of Dictyostelium myosin, in the presence of Mg2+ at low ionic strength, exhibits an average ninefold activation when actin is added." @default.
- W1497478067 created "2016-06-24" @default.
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- W1497478067 date "1974-06-01" @default.
- W1497478067 modified "2023-10-09" @default.
- W1497478067 title "Biochemical and structural studies of actomyosin-like proteins from non-muscle cells" @default.
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- W1497478067 doi "https://doi.org/10.1016/0022-2836(74)90013-8" @default.
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