Expression and rapid one-step purification of biologically active His-tagged factor C by Ni(2+) affinity column chromatography
Publikation: Beitrag in Fachzeitschrift › Forschungsartikel › Beigetragen › Begutachtung
Beitragende
Abstract
Factor C is an unusual extracellular protein capable of inducing cytodifferentiation in certain Streptomyces strains. The protein is produced by Streptomyces griseus 45H at such a low amount that the study of its mode of action was hindered by the shortage of purified protein. We report here the expression of C-terminally hexa-His-tagged factor C in Streptomyces lividans and Escherichia coli. Expression in S. lividans is low while in E. coli it is relatively high, yielding about 5--10 mg of biologically fully active protein per liter culture.
Details
Originalsprache | Englisch |
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Seiten (von - bis) | 223-227 |
Seitenumfang | 5 |
Fachzeitschrift | FEMS microbiology letters |
Jahrgang | 196 |
Ausgabenummer | 2 |
Publikationsstatus | Veröffentlicht - 15 März 2001 |
Peer-Review-Status | Ja |
Extern publiziert | Ja |
Externe IDs
Scopus | 0035868619 |
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ORCID | /0000-0002-2331-2221/work/142242776 |
Schlagworte
Schlagwörter
- Amino Acid Sequence, Amino Acids/analysis, Bacterial Proteins/biosynthesis, Base Sequence, Chromatography, Affinity, Cloning, Molecular, DNA, Bacterial, Escherichia coli, Genes, Bacterial, Histidine/metabolism, Molecular Sequence Data, Recombinant Fusion Proteins/biosynthesis, Streptomyces griseus/genetics, Transformation, Bacterial