Goedde H W, Agarwal D P, Harada S
Enzyme. 1980;25(4):281-6. doi: 10.1159/000459265.
Human liver alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) play an important role in alcohol metabolism. It has been shown that both enzymes are polymorphic and that different variants may be responsible for individual and racial differences in biological sensitivity to ethanol. However, for lack of a suitable peripheral enzyme source, no information is available regarding family data and the mode of inheritance of ADH and ALDH. Using sensitive micro-methods, we report here the detection of these enzymes and their variant forms in human hair root cells. The isozyme pattern of both enzymes obtained by isoelectric focusing from human liver, cultured fibroblast and hair root cell extracts are presented. Several German, Japanese and Vietnamese families were investigated. ALDH was found polymorphic only in Mongoloid populations. Phenotype distribution in a random Japanese population and families suggest a direct relationship between the absence of ALDH I isozyme and alcohol-induced biological sensitivity commonly observed in individuals of Mongoloid origin.
人类肝脏乙醇脱氢酶(ADH)和乙醛脱氢酶(ALDH)在酒精代谢中发挥着重要作用。研究表明,这两种酶都具有多态性,不同的变体可能导致个体和种族对乙醇生物敏感性的差异。然而,由于缺乏合适的外周酶源,关于ADH和ALDH的家族数据及遗传模式尚无相关信息。我们使用灵敏的微量方法,在此报告在人发根细胞中对这些酶及其变体形式的检测。文中呈现了通过等电聚焦从人肝脏、培养的成纤维细胞和发根细胞提取物中获得的这两种酶的同工酶模式。我们对几个德国、日本和越南家庭进行了调查。发现ALDH仅在蒙古人种群体中具有多态性。在一个随机的日本人群体和家庭中的表型分布表明,缺乏ALDH I同工酶与蒙古人种个体中常见的酒精诱导生物敏感性之间存在直接关系。