Abstract
1. 1. Lipoyl dehydrogenase (NADH: lipoamide oxidoreductase, EC 1.6.4.3) and two asparagusate dehydrogenases from asparagus mitochondria were purified by a series of steps, freezing and thawing, sodium dodecylsulfate extraction, and chromatography on Sephadex G-200 and DEAE-cellulose. 2. 2. Lipoyl dehydrogenae was highly specific for α-lipoic acid, which could not be replaced at all by asparagusic acid. Each of the asparagusate dehydrogenases was capable of reducing both asparagusic and α-lipoic acids by using NADH as hydrogen donor. 3. 3. Reduction of α-lipoic acid with NADH by lipoyl dehydrogenase was activated by NAD +, but that of asparagusic acid by asparagusate dehydrogenase was inactivated by NAD +. 4. 4. Lipoyl dehydrogenase and two asparagusate dehydrogenases differed in electrophoretic mobility on polyacrylamide gels.
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