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蜡样芽孢杆菌YUF-4中两种乙酰乙酰辅酶A还原酶的分离及性质

Separation and properties of two acetylacetoin reductases from Bacillus cereus YUF-4.

作者信息

Hosaka T, Ui S, Mimura A

机构信息

Department of Applied Chemistry and Biotechnology, Faculty of Engineering Yamanashi University, Japan.

出版信息

Biosci Biotechnol Biochem. 1999 Jan;63(1):199-201. doi: 10.1271/bbb.63.199.

DOI:10.1271/bbb.63.199
PMID:10052142
Abstract

The separation and purification of two kinds of acetylacetoin reductases (AACRs) from Bacillus cereus YUF-4 were examined. NADPH-linked AACR (AACR I) and NADH-linked AACR (AACR II) were separated from each other by ammonium sulfate fractionation, DEAE-cellulose chromatography, and hydroxyapatite chromatography. The former was purified 3.4-fold with a yield of 10.0%, and the latter was purified 29-fold with a yield of 15.6%. The two enzymes differ from each other in some enzymic properties such as substrate specificity.

摘要

对蜡样芽孢杆菌YUF-4中两种乙酰乙酰辅酶A还原酶(AACRs)进行了分离和纯化研究。通过硫酸铵分级沉淀、DEAE-纤维素层析和羟基磷灰石层析将NADPH连接的AACR(AACR I)和NADH连接的AACR(AACR II)彼此分离。前者纯化了3.4倍,得率为10.0%,后者纯化了29倍,得率为15.6%。这两种酶在底物特异性等一些酶学性质上彼此不同。

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