Arsenate Reductase II. Purine Nucleoside Phosphorylase in the Presence of Dihydrolipoic Acid Is a Route for Reduction of Arsenate to Arsenite in Mammalian Systems

An arsenate reductase has been partially purified from human liver using ion exchange, molecular exclusion, hydroxyapatite chromatography, preparative isoelectric focusing, and electrophoresis. When SDS−β-mercaptoethanol−PAGE was performed on the most purified fraction, two bands were obtained. One...

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Bibliographic Details
Published in:	Chemical research in toxicology Vol. 15; no. 5; pp. 692 - 698
Main Authors:	Radabaugh, Timothy R, Sampayo-Reyes, Adriana, Zakharyan, Robert A, Aposhian, H. Vasken
Format:	Journal Article
Language:	English
Published:	United States American Chemical Society 01-05-2002
Subjects:	Animals Antioxidants - chemistry Arsenite Transporting ATPases Cattle Chromatography Drug Interactions Electrophoresis Humans Ion Pumps - chemistry Ion Pumps - isolation & purification Liver - chemistry Male Mass Spectrometry Multienzyme Complexes - chemistry Multienzyme Complexes - isolation & purification Purine-Nucleoside Phosphorylase - chemistry Purine-Nucleoside Phosphorylase - isolation & purification Thioctic Acid - analogs & derivatives Thioctic Acid - chemistry
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