N-ACETYL-BETA-ALANINE DEACETYLASE IN HOG KIDNEY

被引：20

作者：

FUJIMOTO, D

KOYAMA, T

TAMIYA, N

机构：

[1] Department of Chemistry, Faculty of Science, Tohoku University, Sendai

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1968年 / 167卷 / 02期

关键词：

D O I：

10.1016/0005-2744(68)90220-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

1. (1) An enzyme which catalyzed the hydrolysis of the acetylamino group of N-acetyl-β-alanine was found in mammalian kidney. 2. (2) The enzyme was purified to about 100 fold from hog kidney. 3. (3) The optimal pH of the enzyme was 7.6 Km value for acetyl-β-alanine was 2.5·10-3 M and the enzyme was inhibited by p-chloromercuribenzoate and monoiodo-acetate. 4. (4) Among various acylamino acids tested so far, N-acetyl-β-alanine and to less extent N-acetyl-taurine served as the substrate. 5. (5) A name N-acetyl-β-alanine amidohydrolase (trivial name: N-acetyl-β-alanine deacetylase) was suggested. © 1968.

引用

页码：407 / &