Purification and Properties of Aldose Reductase from Pachysolen tannophilus

概要

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Aldose reductase (EC 1.1.1.21) from Pachysolen tannophilus IFO 1007 was purified 15 fold from the crude enzyme in a yield of 0.9% by pH 5 treatment, protamine sulfate precipitate, ammonium sulfate fractionation, and G-100 gel chromatography. The purified enzyme was entirely homogeneous on disc gel electrophoresis. The optimum pH and temperature were 5-6 and 50℃, and it was stable at pH 6-8 and up to 35℃. Its activity was enhanced slightly by Na_2SO_4,glycylglycine, glutathione, and cysteine, and inhibited remarkably by SH inhibitors such as AgNO_3,HgCl_2,lead acetate and iodoacetate. Its K_m values were determined as follows : 0.97 mM for D-glyceraldehyde, 1.7 mM for DL-glyceraldehyde, 3.5 mM for D-erythrose, 12 mM for D-xylose, 18 mM for L-arabinose, 25 mM for galactose, 33 mM for valeraldehyde, 33 mM for 2-deoxy-D-glucose, 50 mM for propionaldehyde, 67 mM for D-ribose, 200 mM for D-mannose, and 280 mM for acetaldehyde. The enzyme also reduced glucose, L-sorbose, butylaldehyde, and benzaldehyde. Its molecular weight was estimated to be 40,650 by sedimentation equilibrium, 40,000 by SDS polyacrylamide gel electrophoresis and 43,000 by Sephadex G-200 column chromatography.
社団法人日本生物工学会の論文
1987-02-25