来自鲶鱼（Clarias batrachus (L.)）的肝脏精氨酸酶的纯化及性质

Purification and properties of liver arginase from teleostean fish Clarias batrachus (L.).

作者信息

Singh R A, Singh S N

机构信息

Department of Zoology, Banaras Hindu University, Varanasi, India.

出版信息

Arch Int Physiol Biochim. 1990 Dec;98(6):411-9. doi: 10.3109/13813459009114003.

DOI:10.3109/13813459009114003

PMID:1705780

Abstract

Liver arginase of Clarias batrachus has been purified to 56.3-fold employing ammonium sulphate fraction, DEAE-cellulose and CM-cellulose chromatography. Bidirectional polyacrylamide gel electrophoresis shows the presence of two isoenzymes of arginase. The enzyme has a molecular weight of about 87,000 and Km 15.38 mM for L-arginine, optimum pH 9.5 and temperature 37 degrees C. Ornithine and leucine as competitive whereas valine and isoleucine act as non-competitive inhibitors with respect to L-arginine as substrate.

摘要

通过硫酸铵分级沉淀、DEAE-纤维素和CM-纤维素色谱法，将胡子鲶的肝脏精氨酸酶纯化了56.3倍。双向聚丙烯酰胺凝胶电泳显示存在两种精氨酸酶同工酶。该酶的分子量约为87,000，对L-精氨酸的Km为15.38 mM，最适pH为9.5，最适温度为37℃。以L-精氨酸为底物时，鸟氨酸和亮氨酸起竞争性抑制作用，而缬氨酸和异亮氨酸起非竞争性抑制作用。