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- W2019644367 abstract "Abstract l -Myosin and actin have been separated from an actomyosin sol which had interacted with ATP. When an actomyosin sol was treated with ATP and centrifuged at 100, 00 g , the upper 40% of the supernatant contained about 20 to 30% of the total protein. The same actomyosin centrifuged in absence of ATP contained only 2 to 3% of the total protein in the corresponding portion of the supernatant. This protein in the supernatant was identified as l -myosin by the following characteristics: 1. 1. sedimentation constant after the dephosphorylation of ATP; 2. 2. the inhibiting action of Mg ++ on the ATPase activity, reversed by the addition of actin; 3. 3. the disappearance of opalescence at an ionic strength below 0.1 on the addition of ATP and the immediate precipitation after the addition of actin; 4. 4. an ATP sensitivity of zero, changing to one of 100 after the addition of an appropriate amount of actin. The pellet produced on centrifugation yielded actin on extraction with water containing ATP. From these experiments it is concluded that ATP effects the dissociation of an actomyosin sol." @default.
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- W2019644367 date "1956-01-01" @default.
- W2019644367 modified "2023-09-27" @default.
- W2019644367 title "The ultracentrifugal separation of L-myosin and actin in an actomyosin sol under the influence of ATP" @default.
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- W2019644367 doi "https://doi.org/10.1016/0006-3002(56)90439-5" @default.
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