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- W1504516892 abstract "1 Twelve enzymatically active fractions of horse liver alcohol dehydrogenase are demonstrated by starch gel electrophoresis and chromatography on CM- and DEAE-cellulose. A method for the isolation and purification of seven of these multiple molecular forms is described. Their subunit composition is discussed. 2 The isoelectric point was determined for five of the enzymes by the method of isoelectric focusing. 3 Catalytic properties of isoenzyme III (subunit composition AA) are compared with those of isoenzyme V (BB) and enzyme IIc (AA′). Differences are observed with regard to the oxidation of alcohols, the reduction of aldehydes and the pH rate profiles." @default.
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- W1504516892 date "1970-12-01" @default.
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- W1504516892 title "Heterogeneity of Horse Liver Alcohol Dehydrogenase. Purification and Characterization of Multiple Molecular Forms" @default.
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- W1504516892 doi "https://doi.org/10.1111/j.1432-1033.1970.tb01192.x" @default.
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