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• W2045973921 abstract "The hog kidney d-amino acid oxidase used in this study was purified approximately 200-fold. The apooxidase, devoid of FAD, exhibited no glycine oxidase activity and was stable over a period of at least 180 days when maintained at −15°. The limited solubility of phenothiazines at pH 8.3 required that a reliable system be obtained at pH 7.3. That this was accomplished is evidenced by kinetic studies which demonstrated the dependence of enzymic activity on substrate (Km = 1.37 × 10−2 M), FAD (Kƒ = 1.88 × 10−7M), and enzyme concentrations. Chlorpromazine was found to inhibit d-amino acid oxidase in competition with its coenzyme, FAD; the Ki for the reaction being 2.5 × 10−4 M at pH 7.3. The degree of inhibition varied with the method of exposure of the apooxidase, FAD, and chlorpromazine to each other. In addition, this inhibition was found to be a function of the apooxidase protein concentration; i.e. as the protein concentration increased, the extent of inhibition decreased. This was also confirmed by a decreased inhibition when albumin was added to the reaction mixture. Therefore, it is suggested that this nonspecific complexing between chlorpromazine and protein might explain the large number of diverse effects attributed to chlorpromazine and has undoubtedly complicated inhibition studies." @default.
• W2045973921 created "2016-06-24" @default.
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• W2045973921 date "1965-01-01" @default.
• W2045973921 modified "2023-10-16" @default.
• W2045973921 title "Studies of flavin adenine dinucleotide-requiring enzymes and phenothiazines—I. Interactions of chlorpromazine and d-amino acid oxidase" @default.
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• W2045973921 doi "https://doi.org/10.1016/0006-2952(65)90053-5" @default.
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