Temperature-pressure studies on magnesium-activated adenosinetriphosphatase from skeletal muscle.
نویسندگان
چکیده
The effects of pressure, temperature, and pH on the n&\-i@ of purified rabbit skeletal muscle magnesium-activated ATPnsc were measured. The enzyme is rnpidl> and irreversibly inactivated by both temperature and pressure and shows no rvidencc of reversible denaturation. The extent of irreversible inactivation depends on the amount of pressure applied and is largest at the optimum pH of the enzyme.
منابع مشابه
STUDIES ON ADENOSINETRIPHOSPHATASE OF MUSCLE * III. THE LIPOPROTEIN NATURE OF THE MAGNESIUM-ACTIVATED ADENOSINETRIPHOSPHATASE BY W. WAYNE KIELLEYt
In the initial work (1) on the partial isolation and properties of a new magnesium-activated ATPase’ of muscle, it was observed that the enzyme preparations contained a large amount of organic phosphorus, most of which was lipide phosphorus. The relatively small amount of nucleic acid phosphorus could be removed with ribonuclease without impairing the activity of the ATPase. Attempts to separat...
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An ATPase, activated by Na(+) plus K(+) in the presence of Mg(++) and inhibited by ouabain, has been obtained from rat skeletal muscle. Unlike ATPase's with similar properties obtained from other preparations, this ATPase was found only in the fraction containing fragmented sarcoplasmic reticulum. It is suggested that in rat skeletal muscle this ATPase may reside in sarcoplasmic reticulum and n...
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ورودعنوان ژورنال:
- Archives of biochemistry and biophysics
دوره 95 شماره
صفحات -
تاریخ انتشار 1961