Liver cytosolic aldehyde dehydrogenases in rats with different predisposition to induction by phenobarbital. Partial purification and characterization of the enzymes at basal state.
Liver cytosolic aldehyde dehydrogenases were partially purified from rats with different genetic predisposition to induction of aldehyde dehydrogenase activity by phenobarbital. The enzymes were studied at basal state without any pretreatment with an inducer. The main aldehyde dehydrogenases from the non-, high- and intermediate reactor animals could not be differentiated by substrate specificity or thermostability. The enzyme from the non-reactor rats was more resistant to changes of pH and to the inhibitory effects of disulfiram than the enzymes from the high- or intermediate reactors. Immunochemical studies suggested a dissimilarity of these enzymes.
D000444:Aldehyde Dehydrogenase; D000445:Aldehyde Oxidoreductases / Q000096:biosynthesis* / Q000302:isolation & purification; D000818:Animals; D003600:Cytosol / Q000201:enzymology; D004221:Disulfiram / Q000494:pharmacology; D004790:Enzyme Induction; D005260:Female; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000096:biosynthesis* / Q000302:isolation & purification; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D010634:Phenobarbital / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity
D007527:Isoenzymes; D000445:Aldehyde Oxidoreductases; D000444:Aldehyde Dehydrogenase; D004221:Disulfiram; D010634:Phenobarbital