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216.73.217.86
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SCIE SCOPUS
쥐의 뇌 미토콘드리아 알데히드탈수소효소의 정제와 특성에 관한 연구
Purification and Characterization of Rat Brain Mitochondrial Aldehyde Dehydrogenase isozymes
송영한 , 주충노 ( Young Han Song , Chung No Joo )
BMB Reports 24권 6호 625-632(8pages)
UCI I410-ECN-0102-2008-470-002208511

Rat brain mitochondrial aldehyde dehydrogenast isozymes were purified and characterized. There were at last three mitochondrial ALDH isozymes. The soluble ALDH-I was NAD(P)^+ dependent and it has a very low K_m (2.9×10^(-6)M) for succinic semialdehyde but it has a relatively high K_m (10^(-3)M level) for acetaldehyde. However, another soluble ALDH isozyme did not react with succinic semialdehyde. The membrane bound ALDH also has a very low K_m for succinic semialdehyde, however, its reaction rate was slow and its V_(max)/K_m value was only 1/25 that of the soluble ALDH-I. The soluble ALDH-I was significantly inhibited by acetaldehyde. It seemed that ALDH-I might be involved in GABA metabolism related with physiological disturbance caused by over consumption of ethanol.

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