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. 1977 Jan 11;480(1):14-20.
doi: 10.1016/0005-2744(77)90316-3.

Stereospecificity of the hydrogen transfer catalyzed by human placental aldose reductase

H B Feldman, P A Szczepanik, P Havre, R J Corrall, L C Yu, H M Rodman, B A Rosner, P D Klein, B R Landau

Stereospecificity of the hydrogen transfer catalyzed by human placental aldose reductase

H B Feldman et al. Biochim Biophys Acta. .

Abstract

Placental aldose reductase (EC 1.1.1.21) was incubated with glucose in the presence of [4A-2H] NADPH prepared in the oxidation of [2-2H] isocitrate by isocitrate dehydrogenase (EC 1.1.1.42) or [4B-2H] NADPH prepared in the oxidation of [1-2H] glucose-6-phosphate dehydrogenase (EC 1.1.1.49). The sorbitol formed from [4A-2H] NADPH contained deuterium and from [4B-2H] NADPH it did not. Therefore, aldose reductase in an A-type enzyme.

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