| dc.contributor | Wichita State University. Department of Chemistry | en_US |
| dc.contributor.author | Carper, W. Robert | en_US |
| dc.contributor.author | Groutas, William C. | en_US |
| dc.contributor.author | Coffin, D.B. | en_US |
| dc.date.accessioned | 2012-02-06T17:17:04Z | |
| dc.date.available | 2012-02-06T17:17:04Z | |
| dc.date.issued | 1988-01-15 | en_US |
| dc.identifier | 3350116 | en_US |
| dc.identifier | 0376547 | en_US |
| dc.identifier | DK 38853-01 | en_US |
| dc.identifier.citation | Experientia. 1988 Jan 15; 44(1): 29-32. | en_US |
| dc.identifier.issn | 0014-4754 | en_US |
| dc.identifier.uri | http://hdl.handle.net/10057/4390 | |
| dc.description | Full text of this article is not available in SOAR. | en_US |
| dc.description.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. | en_US |
| dc.description.sponsorship | NIDDK NIH HHS | en_US |
| dc.format.extent | 29-32 | en_US |
| dc.language.iso | eng | en_US |
| dc.publisher | Springer | en_US |
| dc.relation.ispartofseries | Experientia | en_US |
| dc.relation.ispartofseries | Experientia | en_US |
| dc.source | NLM | en_US |
| dc.subject | Research Support, Non-U.S. Gov't | en_US |
| dc.subject | Research Support, U.S. Gov't, P.H.S. | en_US |
| dc.subject.mesh | Animals | en_US |
| dc.subject.mesh | Carbohydrate Dehydrogenases/isolation & purification | en_US |
| dc.subject.mesh | Chromatography | en_US |
| dc.subject.mesh | Electrophoresis, Polyacrylamide Gel | en_US |
| dc.subject.mesh | Endoplasmic Reticulum/enzymology | en_US |
| dc.subject.mesh | Glucose 1-Dehydrogenase | en_US |
| dc.subject.mesh | Glucose Dehydrogenases/isolation & purification | en_US |
| dc.subject.mesh | Isoelectric Focusing | en_US |
| dc.subject.mesh | Kinetics | en_US |
| dc.subject.mesh | Liver/enzymology | en_US |
| dc.subject.mesh | NAD/metabolism | en_US |
| dc.subject.mesh | NADP/metabolism | en_US |
| dc.subject.mesh | Swine | en_US |
| dc.subject.mesh | Glucose Dehydrogenases/metabolism | en_US |
| dc.title | Affinity chromatography of glucose dehydrogenase | en_US |
| dc.type | Article | en_US |
| dc.coverage.spacial | Switzerland | en_US |
| dc.description.version | peer reviewed | en_US |
| dc.rights.holder | Copyright © 1988, Birkhäuser Basel | en_US |
