| 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 |