PURIFICATION AND PROPERTIES OF ALPHA-AMINOADIPATE AMINOTRANSFERASE FROM RAT-KIDNEY

被引：2

作者：

MAWAL, MR

DESHMUKH, DR

机构：

[1] Department of Pediatrics, Children’s Hospital of Michigan, Wayne State University, Detroit, MI

来源：

PREPARATIVE BIOCHEMISTRY | 1991年 / 21卷 / 01期

基金：

美国国家卫生研究院;

关键词：

D O I：

10.1080/10826069108021516

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：

Previous studies with rat kidney preparations indicated that alpha-aminoadipate aminotransferase (AadAT) and kynurenine aminotransferase (KAT) activities are associated with a single protein. However, recent studies from our laboratory demonstrated that AadAT and KAT activities belong to two different proteins. AadAT from rat kidney supernatant fraction was purified by affinity chromatography to electrophoretic homogeneity. This rapid and efficient procedure improved the yield and the degree of purification over previously published methods and separated AadAT from KAT. The molecular weight of the enzyme was estimated to be 89,000 by Sephadex G-200 gel filtration chromatography. SDS-PAGE indicated that the enzyme is composed of two apparently identical subunits. Absorption spectra and the kinetic properties of AadAT are reported.

引用

页码：63 / 73

页数：11

共 12 条

[1]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[2] DISC ELECTROPHORESIS .2. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS [J].