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• W2058372849 abstract "Aldehyde dehydrogenase has been purified from rat cornea in a single step. The enzyme is a class 3 aldehyde dehydrogenase. Cornea aldehyde dehydrogenase is a 100-kDa dimer composed of 51-kDa subunits, prefers NADP+ as coenzyme, and preferentially oxidizes benzaldehyde-like aromatic aldehydes as well as medium chain length (4-9 carbons) aliphatic aldehydes. The substrate and coenzyme specificity, immunochemical properties, effect of disulfiram, pH profile, and isoelectric point of cornea aldehyde dehydrogenase are identical to those of tumor-associated aldehyde dehydrogenase, the prototype class 3 enzyme. The substrate and coenzyme preferences are consistent with a role for cornea aldehyde dehydrogenase in the oxidation of a variety of aldehydes generated by lipid metabolism, including lipid peroxidation." @default.
• W2058372849 created "2016-06-24" @default.
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• W2058372849 date "1989-11-01" @default.
• W2058372849 modified "2023-09-26" @default.
• W2058372849 title "Characterization of rat cornea aldehyde dehydrogenase" @default.
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• W2058372849 doi "https://doi.org/10.1016/0003-9861(89)90465-7" @default.
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