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人肝脏醛脱氢酶:在酗酒者和非酗酒者中的亚细胞分布

Human liver aldehyde dehydrogenase: subcellular distribution in alcoholics and nonalcoholics.

作者信息

Meier-Tackmann D, Korenke G C, Agarwal D P, Goedde H W

机构信息

Institute of Human Genetics, University of Hamburg, FRG.

出版信息

Alcohol. 1988 Jan-Feb;5(1):73-80. doi: 10.1016/0741-8329(88)90046-8.

Abstract

Activity assay and isoelectric focusing analysis of human biopsy and autopsy liver specimens showed the existence of two major aldehyde dehydrogenases (ALDH I, ALDH II). Subcellular distribution of these isozymes was determined in autopsy livers from alcoholics and nonalcoholics. Nearly 70% of the total ALDH activity was recovered in the cytosol which contained both the major isozymes. Densitometric evaluation of isozyme bands showed that about 65% of the cytosolic enzyme activity was due to ALDH II and the rest due to ALDH I isozyme. Only about 5% of the total ALDH activity was found in the mitochondrial fraction (70% ALDH I and 30% ALDH II). Significantly reduced total and specific ALDH activities were noted in all the subcellular fractions from cirrhotic liver specimens. Apparently, ALDH I isozyme from cytosol and mitochondria is primarily responsible for the oxidation of small amounts of acetaldehyde normally found in the blood of nonalcoholics after drinking moderate amounts of alcohol. However, in alcoholics who exhibit higher blood acetaldehyde concentrations after drinking alcohol, ALDH II isozyme may be of greater physiological significance.

摘要

对人体活检和尸检肝脏标本进行的活性测定和等电聚焦分析表明,存在两种主要的醛脱氢酶(ALDH I、ALDH II)。在酗酒者和非酗酒者的尸检肝脏中确定了这些同工酶的亚细胞分布。在含有两种主要同工酶的胞质溶胶中,回收了近70%的总ALDH活性。同工酶条带的光密度测定表明,约65%的胞质酶活性归因于ALDH II,其余归因于ALDH I同工酶。仅在线粒体部分中发现约5%的总ALDH活性(70%为ALDH I,30%为ALDH II)。在肝硬化肝脏标本的所有亚细胞部分中,总ALDH活性和特异性ALDH活性均显著降低。显然,胞质溶胶和线粒体中的ALDH I同工酶主要负责氧化非酗酒者饮用适量酒精后血液中通常存在的少量乙醛。然而,对于饮酒后血液乙醛浓度较高的酗酒者,ALDH II同工酶可能具有更大的生理意义。

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