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Journal article
The purification of glutamine synthetase from Azotobacter and other procaryotes by blue sepharose chromatography
BBA - Enzymology, Vol.568(2), pp.428-436
06/06/1979
PMID: 39606
Web of Science ID: WOS:A1979HC86200017
Abstract
We report the facile purification of glutamine synthetase (L-glutamate: ammonia ligase (adenosine 5′-diphosphate-forming), EC 6.3.1.2) in both the adenylylated and unadenylylated form, from Azotobacter vinelandii ATCC 12837. A general affinity column, which used as an affinity ligand Reactive blue 2 dye (Cibacron blue) covalently linked to Agarose, was employed as an efficient first step of purification. Further purification to electrophoretic homogeneity employed DEAE-cellulose chromatography and an additional Affigel chromatographic step. The method was used successfully to prepare glutamine synthetase from Escherichia coli, Rhodopseudomonas sphaeroides and Anabaena sp. strain CA.
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Details
- Title
- The purification of glutamine synthetase from Azotobacter and other procaryotes by blue sepharose chromatography
- Publication Details
- BBA - Enzymology, Vol.568(2), pp.428-436
- Resource Type
- Journal article
- Publisher
- Elsevier B.V
- Number of pages
- 9
- Copyright
- © 1979 Published by Elsevier B.V.
- Identifiers
- WOS:A1979HC86200017; 99380592608206600
- Academic Unit
- Biology; Center for Environmental Diagnostics and Bioremediation ; Hal Marcus College of Science and Engineering
- Language
- English