Solubilization of adenosine triphosphatase from membranes of Escherichia coli: effect of p-aminobenzamidine
نویسندگان
چکیده
منابع مشابه
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چکیده ندارد.
15 صفحه اولSarcoplasmic reticulum. IV. Solubilization of microsomal adenosine triphosphatase.
A soluble adenosine triphosphatase was obtained from skeletal muscle microsomes by extraction with deoxycholate. The Mg++-moderated soluble microsomal ATPase is activated loto ZO-fold by 10m5 M Gaff and inhibited by ethylene glycol bis(P-aminoethyl ether)tetraacetate. Spontaneous formation of microsomal vesicles from solubilized microsomes occurs on removal of deoxycholate by dilution with wate...
متن کاملRegulation by membrane fluidity of the allosteric behavior of the (Ca2)-adenosine triphosphatase from Escherichia coli.
The allosteric properties of the membrane-bound (Ca(2+))-adenosine triphosphatase of an unsaturated fatty acid auxotroph of Escherichia coli were studied in membranes with different fatty acid compositions. The Hill coefficient of the inhibition by Na(+) ranged from 1.4, in the case where the auxotroph was grown with cis-vaccenic acid as supplement, to 2.8 when grown on linolenic acid. The resu...
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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1979
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.138.1.87-91.1979