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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 from human intestine. Because of the differing effects of substrates (p-nitrophenyl phosphate and phenyl phosphate) and their enzymic products (p-nitrophenol and phenol) for L-phenylalanine action on the placental alkaline phosphatase isoenzyme, we suggest that the isoenzyme--inhibitor--substrate complex and the effect of released phosphate on L-phenylalanine inhibition of the isoenzyme activity differ from each other.
T Komoda, and
S Hokari, and
M Sonoda, and
Y Sakagishi, and
T Tamura
January 1954,
The American journal of medical technology,
T Komoda, and
S Hokari, and
M Sonoda, and
Y Sakagishi, and
T Tamura
February 2020,
Analytica chimica acta,
T Komoda, and
S Hokari, and
M Sonoda, and
Y Sakagishi, and
T Tamura
January 1960,
Le Scalpel,
T Komoda, and
S Hokari, and
M Sonoda, and
Y Sakagishi, and
T Tamura
January 1972,
Biologie et gastro-enterologie,
T Komoda, and
S Hokari, and
M Sonoda, and
Y Sakagishi, and
T Tamura
August 1967,
Clinica chimica acta; international journal of clinical chemistry,
T Komoda, and
S Hokari, and
M Sonoda, and
Y Sakagishi, and
T Tamura
October 1971,
Biochemical and biophysical research communications,
T Komoda, and
S Hokari, and
M Sonoda, and
Y Sakagishi, and
T Tamura
May 2019,
Analytical biochemistry,
T Komoda, and
S Hokari, and
M Sonoda, and
Y Sakagishi, and
T Tamura
June 1972,
Clinical chemistry,
T Komoda, and
S Hokari, and
M Sonoda, and
Y Sakagishi, and
T Tamura
May 1975,
Analytical biochemistry,
T Komoda, and
S Hokari, and
M Sonoda, and
Y Sakagishi, and
T Tamura
November 1971,
The Histochemical journal,
