Purification and characterization of aldehyde dehydrogenase from rat liver mitochondria.

Abstract

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.

Cite this paper

@article{Senior1988PurificationAC, title={Purification and characterization of aldehyde dehydrogenase from rat liver mitochondria.}, author={Dave Senior and Ching Sung Tsai}, journal={Archives of biochemistry and biophysics}, year={1988}, volume={262 1}, pages={211-20} }