title: Affinity chromatography of glucose dehydrogenase.
abstract: 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.
authors.affiliation: Department of Chemistry, Wichita State University, Kansas 67208.
authors.forename: W R
authors.initials: WR
authors.lastname: Carper
authors.forename: W C
authors.initials: WC
authors.lastname: Groutas
authors.forename: D B
authors.initials: DB
authors.lastname: Coffin
mesh_terms: D000818:Animals; D002237:Carbohydrate Dehydrogenases / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004721:Endoplasmic Reticulum / Q000201:enzymology; D042843:Glucose 1-Dehydrogenase; D005948:Glucose Dehydrogenases / Q000302:isolation & purification* / Q000378:metabolism; D007525:Isoelectric Focusing; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D013552:Swine
chemical_list: D009243:NAD; D009249:NADP; D002237:Carbohydrate Dehydrogenases; D005948:Glucose Dehydrogenases; D042843:Glucose 1-Dehydrogenase