Purification and characterization of nadph-linked aldehyde reductase from pig brain
NADPH-linked aldehyde reductase was purified 750- fold with an 18% yield from pig brain. The enzyme was shown to catalyze both the reduction of aromatic and aliphatic aldehydes and the oxidation of aromatic and aliphatic alcohols. Although aldehyde reductase catalyzes the same reactions as alcohol dehydrogenase, these two enzymes can easily be distinguished from each other by their response to pyrazole and barbiturates. Aldehyde reductase is inhibited by barbiturates but not by pyrazole. The inverse is true for alcohol dehyrogenase. Aldehyde reductase uses the NADPH/NADP cofactor system as opposed to the NADH/NAD system of alcohol dehydrogenase. A study of aldehyde reductase's response to inhibitors indicates that it is inhibited noncompetitively by barbiturates, competitively by chlorpromazine hydrochloride, and uncompetitively by acetaldehyde. Inhibition by metal chelating agents, 1,10-orthophenanthroline, and sulfide implicates the involvement of a metal ion in the catalytic process. Sulfhydryl involvement is suggested by inhibition by iodoacetate.
College and Department
Chemistry and Biochemistry
BYU ScholarsArchive Citation
Susa, John Baptist, "Purification and characterization of nadph-linked aldehyde reductase from pig brain" (1973). Theses and Dissertations. 8364.
Enzymes, Amines, Aldehydes, Swine, Brain