Human skeletal alkaline phosphatase. Kinetic studies including pH dependence and inhibition by theophylline.
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منابع مشابه
Human skeletal alkaline phosphatase. Kinetic studies including pH dependence and inhibition by theophylline.
The skeletal isoenzyme of human alkaline phosphatase was partially purified from the serum of a patient with Paget’s disease. The pH dependence of the reaction with p-nitrophenyl phosphate (PNPP) suggests that either the reaction mechanism involves 2 dissociable residues on the enzyme (8.75 > pK1 > 8.2; 9.35 > pKz > 8.75), or that the monoanion is the active form of the phosphoryl substrate. In...
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The degree of inhibition of rat intestinal alkaline phosphatase by L-phenylalanine was highly pa-dependent and varied from 0 to 66% within a pH range of ‘7.8 to 10.4, exhibiting a peak at pH 9.2 and 8.7 for phenylphosphate and /3glycerophosphate, respectively. Vm,, was also a function of pH with and without the inhibitor. Rat intestinal alkaline phosphatase exhibited maximum enzyme activity at ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1980
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)85548-5