Abstract
A form of human liver alcohol dehydrogenase previously identified on starch gel electrophoresis as the anodic band (Li, T.-K. and Magnes, L.J. Biochem. Biophys. Res. Commun. 63, 202, 1975) has now been separated from the other molecular forms of the enzyme by affinity chromatography on 4-[3-(N-6-aminocaproyl)-aminopropyl]-pyrazole-Sepharose and purified to homogeneity on Agarose-hexane-AMP. Its physical properties are similar to those of other molecular forms already known, suggesting that they may be related. In contrast to other forms, the anodic species is inactive towards methanol, and its K M for ethanol is as much as 100 times that of the other forms. This anodic form of alcohol dehydrogenase may contribute significantly to alcohol elimination in man, particularly at high alcohol concentrations when the other enzyme species are saturated.
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