PURIFICATION FROM HUMAN-BRAIN AND SOME PROPERTIES OF 2 NADPH-LINKED ALDEHYDE REDUCTASES WHICH REDUCE SUCCINIC SEMI-ALDEHYDE TO 4-HYDROXYBUTYRATE

被引:91
作者
CASH, CD
MAITRE, M
MANDEL, P
机构
[1] Centre de Neurochimie du C.N.R.S, Strasbourg, 67085, rue Humann
关键词
aldehyde reductase; gamma‐hydroxybutyrate; human brain; succinic semialdehyde;
D O I
10.1111/j.1471-4159.1979.tb05261.x
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
Abstract— Two NADPH‐linked aldehyde reductases (alcohol:NADP+oxidoreductase, EC 1.1.1.2) capable of reducing succinic semialdehyde to the anaesthetic Chydroxybutyrate have been purified from human brain to electrophoretic homogeneity. The first of these enzymes, which is typical of its category, is not specific for succinic semialdehyde and can reduce some aromatic aldehydes at a high rate. It is a monomer of molecular weight about 45,000 and is strongly inhibited by various hypnotics and anticonvulsants. The second enzyme is, in contrast, fairly specific for succinic semialdehyde. It is a dimer of molecular weight about 90,000 and is not inhibited by the hypnotics and anticonvulsants which inhibit the first enzyme. It is thus different from previously described aldehyde reductases from human brain. Copyright © 1979, Wiley Blackwell. All rights reserved
引用
收藏
页码:1169 / 1175
页数:7
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