Abstract
Glycerol dehydrogenase activity is found in several mammalian tissues. This chapter describes the assay method of glycerol dehydrogenase isolated from the rabbit muscle. The enzyme catalyzes the nicotinamide adenine dinucleotide phosphate kinase (NADP + )-linked reduction of a wide variety of aldoses and aliphatic and aromatic aldehydes. It is similar to both NADP L-hexonate dehydrogenase and aldose reductase. Glycerol dehydrogenase activity from the rabbit muscle is because of two enzymes, both of which are different from aldehyde reductase. One of the rabbit muscle enzymes is immunologically identical with aldose reductase from the rabbit lens. Glycerol dehydrogenase activity is assayed spectrophotometrically by determining the decrease in the absorbance of nicotinamide adenine dinucleotide phosphate dehydrogenase (NADPH) at 340 nm. The reaction is carried out at 25°C in a Beckman 25 double-beam recording spectrophotometer. The scale is expanded to give a full scale expansion of 0.25. The chapter discusses the steps involved in the purification procedure of glycerol dehydrogenase. It also presents the diethylaminoethyl (DEAE)-Sephacel chromatography of glycerol dehydrogenases obtained from rabbits.
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