Preparation of a highly active alcohol apo-dehydrogenase from yeast

Abstract

It is generally recognized that an active dehydrogenase system consists of three principal components: (1) an apo-dehydrogenase, the non-dializable and thermo-labile colloidal carrier, protein in nature; (2) a co-enzyme, crystalloidal and comparatively thermostable; and (3) a flavo-protein, capable of reversible oxidations and reductions. Euler and others have advanced the view that the specificity of dehydrogenases is intimately associated with the specific protein or proteins constituting the apo-dehydrogenase, the isolation of which in a state of integral purity and high activity is necessary for an elucidation of the groups responsible for the enzymic activity. With this end in view, we have commenced a study of the isolation and purification of the alcohol apo-dehydrogenase from bottom yeast.