Racial differences in biological sensitivity to ethanol: the role of alcohol dehydrogenase and aldehyde dehydrogenase isozymes.
Electrophoretic and kinetic studies of autopsy liver specimens from individuals of different racial groups revealed a polymorphism in alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH). About 85% of the Japanese livers had an atypical ADH and 52% of the livers an unusual ALDH. Only 13% of German liver specimens had the atypical ADH and none showed the unusual form of ALDH which lacks in the isozyme with low Km for acetaldehyde. Using hair roots as the source of ADH and ALDH, individuals showing sensitivity to ethanol were examined. Data on the distribution of phenotypes in random European and Japanese population as well as family studies suggest a direct relationship between the lack of low Km isozyme of ALDH and alcohol-induced biological sensitivity. Our findings suggest that the alcohol sensitivity quite common in individuals of Mongoloid origin might be due to delayed oxidation of acetaldehyde by an unusual type of ALDH.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000445:Aldehyde Oxidoreductases / Q000378:metabolism*; D044466:Asian People; D004592:Electrophoresis, Starch Gel; D000431:Ethanol / Q000494:pharmacology*; D005860:Germany, West; D006197:Hair / Q000201:enzymology; D006801:Humans; D007527:Isoenzymes / Q000378:metabolism*; D007564:Japan; D008099:Liver / Q000201:enzymology; D010375:Pedigree; D010641:Phenotype; D044465:White People
D007527:Isoenzymes; D000431:Ethanol; D000429:Alcohol Oxidoreductases; D000445:Aldehyde Oxidoreductases