YAKUGAKU ZASSHI
Online ISSN : 1347-5231
Print ISSN : 0031-6903
ISSN-L : 0031-6903
Carboxypeptidase CN(第3報)エステラーゼ活性
久保田 幸穂庄司 省三船越 崇行植木 寛
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1974 年 94 巻 8 号 p. 964-969

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A colorimetric method for the determination of methanol with chromotropic acid was applied to the assay of the esterolytic activity of carboxypeptidase CN (CPase CN) with p-toluenesulfonyl-L-arginine methyl ester (TAME) as substrate. The method was found to be sensitive and useful for the determination of the esterolytic activity of CPase CN. p-Nitrophenyl acetate, another substrate for esterase assay, was also used for comparison. The specific activity of CPase CN was 0.60 unit/mg protein for TAME and 0.06 unit/mg protein for p-nitrophenyl acetate. The optimal pH and temperature for the esterolytic action of CPase CN were pH 5.5 and 50°, respectively. Both carboxypeptidase and esterolytic activities were inhibited by diisopropylfluorophosphate (10-3M) and HgCl2 (10-4 M). The activities were also decreased on reaction with 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide and glycine methyl ester. Preincubation of CPase CN with TAME (50 or 100 mM) decreased the hydrolysis rate of Z-Glu -Phe by the enzyme.

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© by the PHARMACEUTICAL SOCIETY OF JAPAN
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