Characterization of rat cornea aldehyde dehydrogenase.
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.
Evces
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Department of Biology, University of Alabama, Tuscaloosa.
Lindahl
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R
D000444:Aldehyde Dehydrogenase / Q000037:antagonists & inhibitors / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D015153:Blotting, Western; D003315:Cornea / Q000201:enzymology*; D004221:Disulfiram / Q000494:pharmacology; D005136:Eye Proteins / Q000302:isolation & purification; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009249:NADP; D051381:Rats; D013379:Substrate Specificity
D005136:Eye Proteins; D009249:NADP; D000444:Aldehyde Dehydrogenase; D004221:Disulfiram