Expression and rapid one-step purification of biologically active His-tagged factor C by Ni(2+) affinity column chromatography
Research output: Contribution to journal › Research article › Contributed › peer-review
Contributors
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
Original language | English |
---|---|
Pages (from-to) | 223-227 |
Number of pages | 5 |
Journal | FEMS microbiology letters |
Volume | 196 |
Issue number | 2 |
Publication status | Published - 15 Mar 2001 |
Peer-reviewed | Yes |
Externally published | Yes |
External IDs
Scopus | 0035868619 |
---|---|
ORCID | /0000-0002-2331-2221/work/142242776 |
Keywords
Keywords
- 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