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. 1989 Dec 1;264(2):403–407. doi: 10.1042/bj2640403

Isolation from pig lens of two proteins with dihydrodiol dehydrogenase and aldehyde reductase activities.

A Hara 1, T Harada 1, M Nakagawa 1, K Matsuura 1, T Nakayama 1, H Sawada 1
PMCID: PMC1133595  PMID: 2690827

Abstract

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.

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Selected References

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