Abstract
An aliphatic l-α-hydroxyacid oxidase present in a light mitochondrial fraction of rat liver cells was purified some 600-fold. At this stage the enzyme had a purity of 67%. The enzyme was still contaminated with catalase, and its absorption spectrum did not show a typical flavoprotein curve. Absorbance at 460 mμ was rapidly reduced by the addition of dithionite in air or of substrate during anaerobiosis. The difference spectrum of the reduced enzyme suggested that the enzyme is a flavoprotein. Spectrophotometry and paper chromatography of the extract of the enzyme after heat treatment indicated that the prosthetic group is FMN.
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