Hara A, Harada T, Nakagawa M, Matsuura K, Nakayama T, Sawada H
Department of Biochemistry, Gifu Pharmaceutical University, Japan.
Biochem J. 1989 Dec 1;264(2):403-7. doi: 10.1042/bj2640403.
Dimeric and monomeric proteins containing dihydrodiol dehydrogenase and aldehyde reductase activities were purified from pig lens. The dimeric enzyme of Mr 65,000 specifically oxidized the trans-dihydrodiols of naphthalene and benzene with NADP+ as a strict cofactor, and reduced alpha-diketones, aromatic aldehydes and glyceraldehyde with NADPH as a cofactor. The monomeric enzyme of Mr 35,000, although identical with aldose reductase, oxidized the trans-dihydrodiol of naphthalene at a pH optimum of 7.6. These results suggest that the two enzymes are involved in the pathogenesis of naphthalene cataract.
从猪晶状体中纯化出了具有二氢二醇脱氢酶和醛还原酶活性的二聚体和单体蛋白质。分子量为65,000的二聚体酶以NADP⁺作为严格的辅因子特异性氧化萘和苯的反式二氢二醇，并以NADPH作为辅因子还原α-二酮、芳香醛和甘油醛。分子量为35,000的单体酶虽然与醛糖还原酶相同，但在最适pH 7.6时氧化萘的反式二氢二醇。这些结果表明这两种酶参与了萘性白内障的发病机制。
