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The P-Nitrophenyl Phosphatase Activity of Ubiquitin From Bovine Erythrocytes

The P-Nitrophenyl Phosphatase Activity of Ubiquitin From Bovine Erythrocytes

N Taniguchi, H Matsumoto

Comp Biochem Physiol B. 1985;81(3):587-90.

PMID: 2992874

Abstract:

Ubiquitin, a unique protein with esterase and carbonic anhydrase activity, has been found to have also a p-nitrophenyl phosphatase activity. This phosphomonoesterase activity of ubiquitin has an acidic pH optimum; its true substrate appears to be the phosphomonoanion, with a Km of 1.8 X 10(-3) M. It is competitively inhibited by the typical acid phosphatase inhibitors, arsenate (Ki = 1.3 X 10(-3) M), molybdate (Ki = 1.2 X 10(-6) M), and phosphate (Ki = 1.4 X 10(-3) M). These inhibitors have no effect on the CO2 hydration and p-nitrophenyl acetate esterase activities of the ubiquitin. Acetazolamide slightly inhibited the p-nitrophenyl phosphatase activity.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP79586224	Ubiquitin from bovine erythrocytes		79586-22-4	Price

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