Purification of alditol:NADP oxidoreductase from human placenta

Alditol:NADP oxidoreductase has been isolated and purified to homogeneity from human placenta. The enzyme has substrate specficities similar to those reported for partially purified alditol:NADP oxidoreductase from other mammalian species and has an approximate molecular weight of 39,000. The isolat...

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Veröffentlicht in:	Biochemical and biophysical research communications 1972-06, Vol.47 (6), p.1473-1479
Hauptverfasser:	Clements, Rex S., Winegrad, Albert I.
Format:	Artikel
Sprache:	eng
Schlagworte:	Alcohol Oxidoreductases - antagonists & inhibitors Alcohol Oxidoreductases - isolation & purification Ammonium Sulfate Calcium Phosphates Centrifugation, Zonal Chemical Precipitation Chromatography, DEAE-Cellulose Chromatography, Gel Electrophoresis, Disc Enzyme Activation Female Glutarates Humans Hydroxybutyrates Isoelectric Focusing Lithium Molecular Weight Monosaccharides NADP Placenta - enzymology Pregnancy Sodium Chloride Structure-Activity Relationship Sugar Alcohols Sulfates
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Zusammenfassung:	Alditol:NADP oxidoreductase has been isolated and purified to homogeneity from human placenta. The enzyme has substrate specficities similar to those reported for partially purified alditol:NADP oxidoreductase from other mammalian species and has an approximate molecular weight of 39,000. The isolation of alditol:NADP oxidoreductase from human placenta supports the view that fructose synthesis from glucose in this tissue proceeds via the intermediate formation of sorbitol.
ISSN:	0006-291X 1090-2104
DOI:	10.1016/0006-291X(72)90238-0