ISSN:
1573-4927
Keywords:
alcohol dehydrogenase
;
polymorphism
;
isozyme
;
electrophoresis
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
Notes:
Abstract New molecular forms of human liver alcohol dehydrogenase (ADH), collectively designated ADHIndianapolis (ADHInd), were recently discovered in 29% of liver specimens from Black Americans [Bosron, W. F., Li, T.-K., and Vallee, B. L. (1981). Proc. Natl. Acad. Sci. USA 77:5784]. Three different ADHInd phenotypes have now been identified by starch gel electrophoresis, and four ADHInd enzyme forms isolated by affinity and ion-exchange chromatography. The most cathodic ADHInd form has a single pH optimum at 7.0 for ethanol oxidation and is a homodimer of a newly discovered subunit, as evidenced by dissociation-recombination studies. The remaining three purified ADHInd forms have dual pH optima for ethanol oxidation at 7.0 and 10.0 and generate two new bands on starch gel electrophoresis after dissociation-recombination. They appear to be heterodimers of this new subunit with the known subunits, α, β1, and γ1. Based on the occurrence of these four ADHInd isozymes and isozymes containing β1 subunits in the homogenate supernatants of 135 livers, we conclude that ADHInd results from polymorphism at the ADH 2locus, with the variant ADH 2 Ind allele coding for the βInd subunit. The frequency of ADH 2 Ind was 0.16 in Black Americans, and this allele was not observed in any of the 63 livers from White Americans. The frequency of the ADH 3 1 and ADH 3 2 alleles also differed in these two populations.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00498920
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