Abstract
AMONG several substances examined in our laboratory for their influence on the activity of D-amino-acid oxidase, chlorpromazine (N-(3′-dimethylaminopropyl)-3-chlorophenothiazine hydrochloride) was found to be a powerful inhibitor of this enzyme. The inhibitory mechanism was investigated using a purified oxidase enzyme system and Warburg manometer, and the kinetic study carried out. D-Amino-acid oxidase protein was prepared from hog kidney by the method of Negelein and Bromel1. Each enzyme system consisted of apo-enzyme (protein E), 1.6 × 10−7 mole of flavin adenine dinucleotide prepared by the method of Yagi et al. 2, 6.25 × 10−2 mole of D-alanine. Amounts of chlorpromazine (supplied by Rhone-Poulenc-Specia) ranging from 2 × 10−5 to 4 × 10−6 mole were added to these enzyme systems.
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