
Porcine liver beta-D-glucose dehydrogenase, a multi-functional protein, has been purified to apparent homogeneity. The enzyme has been separated from the endoplasmic reticulum using Triton X-114 and further purified using NAD to release glucose dehydrogenase from a NADP-linked sepharose column. The purified enzyme is capable of producing both NADH and NADPH in vivo as indicated by kinetic studies.
Electrophoresis, 570, Swine, Glucose Dehydrogenases, 610, Research Support, Endoplasmic Reticulum, P.H.S, Chromatography, Affinity, Glucose Dehydrogenases/isolation & purification, Animals, Non-U.S. Gov't, Chromatography, Polyacrylamide Gel, Endoplasmic Reticulum/enzymology, Liver/enzymology, Glucose 1-Dehydrogenase, NADP/metabolism, NAD, Glucose Dehydrogenases/metabolism, Kinetics, Liver, Carbohydrate Dehydrogenases/isolation & purification, Carbohydrate Dehydrogenases, Electrophoresis, Polyacrylamide Gel, U.S. Gov't, NAD/metabolism, Isoelectric Focusing, NADP
Electrophoresis, 570, Swine, Glucose Dehydrogenases, 610, Research Support, Endoplasmic Reticulum, P.H.S, Chromatography, Affinity, Glucose Dehydrogenases/isolation & purification, Animals, Non-U.S. Gov't, Chromatography, Polyacrylamide Gel, Endoplasmic Reticulum/enzymology, Liver/enzymology, Glucose 1-Dehydrogenase, NADP/metabolism, NAD, Glucose Dehydrogenases/metabolism, Kinetics, Liver, Carbohydrate Dehydrogenases/isolation & purification, Carbohydrate Dehydrogenases, Electrophoresis, Polyacrylamide Gel, U.S. Gov't, NAD/metabolism, Isoelectric Focusing, NADP
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