ATPase activity of purified and reconstituted P-glycoprotein from Chinese hamster ovary cells.
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چکیده
منابع مشابه
ATPase activity of purified and reconstituted P-glycoprotein from Chinese hamster ovary cells.
P-glycoprotein was purified from multidrug-resistant Chinese hamster ovary CHRB30 cells by a combination of anion exchange and immunoaffinity chromatography. The P-glycoprotein was about 90% pure and had a Vmax for ATP hydrolysis in detergent solution of 321 nmol/min/mg with a Km of 0.94 mM. The ATPase activity was inhibited by low concentrations of vanadate and N-ethylmaleimide, but unaffected...
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P-Glycoprotein (Pgp) was isolated from CHRC5 membranes by selective detergent extraction and further purified by lentil lectin affinity chromatography. The purified product displayed a very high basal ATPase activity (1.65 mumol/min per mg protein in the absence of added drugs or lipids) with an apparent Km for ATP of 0.4 mM. There was no evidence of cooperativity, suggesting that the two ATP s...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1994
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)41923-5