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- W2258708994 abstract "1. A simple procedure involving repeated washings of actomyosin, extracted as the complex from myofibrils (natural actomyosin) at ionic strength less than 0.002, is described for the preparation of a desensitized actomyosin. 2. The Mg(2+)-activated adenosine triphosphatase of natural actomyosin was markedly inhibited by ethylenedioxybis(ethyleneamino)tetra-acetic acid, whereas that of the desensitized actomyosin was unaffected. 3. The activity of the Ca(2+)-activated adenosine triphosphatase of natural actomyosin was generally lower than that of the Mg(2+)-activated adenosine triphosphatase, whereas in the desensitized actomyosin the difference between the activities was considerably less. In both natural and desensitized actomyosin the adenosine-triphosphatase activities in the presence of Mg(2+) were similar. 4. The conversion of the natural into the desensitized actomyosin was accompanied by the removal of a protein fraction containing the factors responsible for the sensitivity to ethylenedioxybis(ethyleneamino)tetra-acetic acid and for modifying the Ca(2+)-activated adenosine triphosphatase. When added to a desensitized actomyosin this fraction effected a reversal to the natural form. The recombination was facilitated by increasing the ionic strength of the medium. The two factors showed different stabilities to heat and tryptic digestion." @default.
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- W2258708994 date "1967-07-01" @default.
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- W2258708994 title "The adeonosine-triphosphatase activity of desensitized actomyosin" @default.
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- W2258708994 doi "https://doi.org/10.1042/bj1040263" @default.
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