Heterogeneity of Horse Liver Alcohol Dehydrogenase

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.