Sato S, Kador P F
National Eye Institute, Bethesda, Maryland 20892.
Invest Ophthalmol Vis Sci. 1989 Jul;30(7):1618-22.
Aldehyde reductase (E.C. 1.1.1.2) has been purified to apparent homogeneity from rat lens and its properties have been compared to those of both rat lens aldose reductase and rat kidney aldehyde reductase. The purification was accomplished by ammonium sulfate fractionation, Sephadex G-75 chromatography, affinity chromatography on Amicon Matrex Gel Orange A and chromatofocusing. The purified enzyme is distinct from rat lens aldose reductase but appears similar to rat kidney aldehyde reductase in molecular weight, immunological properties and substrate specificities. Rat lens aldehyde reductase is inhibited by a number of aldose reductase inhibitors; however, its susceptibility to inhibition is more similar to rat kidney aldehyde reductase than to rat lens aldose reductase.
醛还原酶(E.C. 1.1.1.2)已从大鼠晶状体中纯化至表观均一,其性质已与大鼠晶状体醛糖还原酶和大鼠肾脏醛还原酶的性质进行了比较。纯化过程通过硫酸铵分级分离、Sephadex G - 75色谱、Amicon Matrex Gel Orange A亲和色谱和色谱聚焦完成。纯化后的酶与大鼠晶状体醛糖还原酶不同,但在分子量、免疫特性和底物特异性方面与大鼠肾脏醛还原酶相似。多种醛糖还原酶抑制剂可抑制大鼠晶状体醛还原酶;然而,其对抑制的敏感性与大鼠肾脏醛还原酶更为相似,而非大鼠晶状体醛糖还原酶。