Inhibition of alkaline phosphatase by L-phenylalanine

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On the mechanism of inhibition of intestinal alkaline phosphatase by L-phenylalanine. I. Kinetic studies.

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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On the Mechanism of Inhibition of Intestinal Alkaline Phosphatase by L-Phenylalanine

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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The inhibition of alkaline phosphatase by beryllium.

Recent clinical reports of pulmonary disease occurring in workers in the beryllium industry have stimulated new interest in the biochemical action of this element (for a complete bibliography, see (1)). Although it has not been possible to produce in animals pathological conditions identical with those Eeen in beryllium workers, experimental administration of beryllium and its compounds has res...

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Inhibition of alkaline phosphatase by oestradiol phosphates.

specific biological activity when isolated from different species may differ chemically. The haemo. globins are an example of this (Porter & Sanger, 1948), and it is clear that some variation in structure may occur in such a series of compounds without the specific action being greatly modified. From solubility studies, Desreux & Herriott (1939) postulated the existence of at least two componen...

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L-Phenylalanine inhibition of human alkaline phosphatases with p-nitrophenyl phosphate as substrate.

With p-nitrophenyl phosphate as the substrate, there reportedly is no organ-specific inhibition of alkaline phosphatase (EC 3.1.3.1) activity by L-phenylalanine. However, we found that at pH 10.0, with p-nitrophenyl phosphate as the substrate, L-phenylalanine obviously inhibits the alkaline phosphatase isoenzyme from human placenta, whereas there is little if any inhibition of the isoenzyme fro...

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ژورنال

عنوان ژورنال: Biochemical Journal

سال: 1970

ISSN: 0306-3283

DOI: 10.1042/bj1160543