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鸡肌肉中L-甘油脱氢酶的纯化及某些性质

Purification and some properties of L-glycol dehydrogenase from hen's muscle.

作者信息

Bernardo A, Burgos J, Martín R

出版信息

Biochim Biophys Acta. 1981 May 14;659(1):189-98. doi: 10.1016/0005-2744(81)90283-7.

DOI:10.1016/0005-2744(81)90283-7
PMID:7018582
Abstract
  1. An enzyme which catalyzes the NAD(P)H-linked reversible reduction of uncharged vicinal dicarbonyls and alpha-hydroxycarbonyls to L-(+)-glycols has been purified from hen's muscle. This enzyme has not been previously described. 2. According to the rules of the I.U.P.A.C.-I.U.B. Enzymes Commission, the systematic name of L-(+)-glycol:NAD(P) oxidoreductase and the trivial name of L-glycol dehydrogenase are proposed for the enzyme. 3. Three forms of this enzyme differing in pI have been isolated; two forms, which together represent about 90% of total recovered activity, and electrophoretically pure. 4. Molecular weight, pH profiles and affinity for substrates are also described.
摘要
  1. 从母鸡肌肉中纯化出一种酶,它催化无电荷的邻二羰基化合物和α-羟基羰基化合物以NAD(P)H为媒介可逆还原为L-(+)-二醇。此前尚未描述过这种酶。2. 根据国际纯粹与应用化学联合会-国际生物化学联合会酶委员会的规则,提议将该酶的系统名称定为L-(+)-二醇:NAD(P)氧化还原酶,通用名称定为L-二醇脱氢酶。3. 已分离出三种等电点不同的该酶形式;其中两种形式共同代表了约90%的总回收活性,且为电泳纯品。4. 还描述了该酶的分子量、pH曲线和对底物的亲和力。

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引用本文的文献

1
Purification and characterization of diacetyl-reducing enzymes from Staphylococcus aureus.金黄色葡萄球菌中双乙酰还原酶的纯化与特性分析
Biochem J. 1988 Apr 15;251(2):461-6. doi: 10.1042/bj2510461.