Purification and characterization of aldehyde dehydrogenase from rat liver mitochondria.
Nicotinamide adenine dinucleotide- and nicotinamide adenine dinucleotide phosphate-dependent dehydrogenase activities from rat liver mitochondria have been copurified to homogeneity using combined DEAE, Sepharose, and affinity chromatographic procedures. The enzyme has a native molecular weight of 240,000 and subunit molecular weight of 60,000. The enzyme is tetrameric consisting of four identical subunits as revealed by electrophoresis and terminal analyses. A partial summary of physical properties is provided. The amino acid composition by acid hydrolysis is reported. Specific activities for various NAD(P)+ analogs and alkanal substrates were compared. The action of the effectors chloral hydrate, disulfiram, diethylstilbestrol, and Mg2+ and K+ ions were also investigated.
Senior
D J
DJ
Ottawa-Carleton Chemistry Institute, Carleton University, Ontario, Canada.
Tsai
C S
CS
D000444:Aldehyde Dehydrogenase / Q000302:isolation & purification*; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D007525:Isoelectric Focusing; D008930:Mitochondria, Liver / Q000201:enzymology*; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains
D000596:Amino Acids; D009243:NAD; D009249:NADP; D000444:Aldehyde Dehydrogenase