Branlant G
Eur J Biochem. 1982 Dec;129(1):99-104. doi: 10.1111/j.1432-1033.1982.tb07026.x.
Two monomeric NADPH enzymes from pig lens, an aldehyde reductase and an aldose reductase, have been characterized. The aldose reductase is obtained in a pure form. The aldehyde reductase, usually called hexonate dehydrogenase, is the same protein as that was recently isolated from pig liver [Branlant, G. and Biellmann, J.F. (1980) Eur. J. Biochem. 105, 611-621]. The aldose reductase is shown to have a number of properties in common with the aldehyde reductase, namely its physico-chemical properties, its tendency to be inhibited by quercitine derivatives and its substrate specificity. These two enzymes differ in their immunological properties. Only aldose reductase has a reactive Cys residue, localized in or near the substrate binding site. In contrast to that shown for aldehyde reductase [Branlant, G. et al. (1981) Eur. J. Biochem. 116, 505-512; Branlant, G. (1982) Eur. J. Biochem. 121, 407-411], no anion-recognition sites are in the substrate binding site of aldose reductase. The fact that also sugars are substrates for aldose reductase support the idea that this enzyme is implicated in the formation of sugar cataract as suggested by Kinoshita, J.H. et al. [J. Am. Med. Ass. 246, 257-261 (1981)]. Pig lens aldose reductase does not show homotropic cooperative effects with respect to either substrate or coenzyme.
已对猪晶状体中的两种单体NADPH酶——一种醛还原酶和一种醛糖还原酶进行了特性分析。醛糖还原酶以纯形式获得。醛还原酶，通常称为己糖酸脱氢酶，与最近从猪肝中分离出的蛋白质相同[布兰兰特，G.和比尔曼，J.F.（1980年）《欧洲生物化学杂志》105卷，611 - 621页]。醛糖还原酶显示出与醛还原酶有许多共同特性，即其物理化学性质、被槲皮素衍生物抑制的倾向及其底物特异性。这两种酶在免疫特性上有所不同。只有醛糖还原酶有一个位于底物结合位点内或附近的活性半胱氨酸残基。与醛还原酶所显示的情况不同[布兰兰特，G.等人（1981年）《欧洲生物化学杂志》116卷，505 - 512页；布兰兰特，G.（1982年）《欧洲生物化学杂志》121卷，407 - 411页]，醛糖还原酶的底物结合位点没有阴离子识别位点。糖也是醛糖还原酶的底物这一事实支持了如下观点，即正如木下，J.H.等人所提出的[《美国医学协会杂志》246卷，257 - 261页（1981年）]，该酶与糖性白内障的形成有关。猪晶状体醛糖还原酶在底物或辅酶方面均未表现出同促协同效应。
