Plasmid pGEX-5T: An alternative system for expression and purification of recombinant proteins
β Scribed by Heike Berthold; Brigitte Frorath; Mirko Scanarini; Charles C. Abney; Bruno Ernst; Wolfgang Northemann
- Publisher
- Springer Netherlands
- Year
- 1992
- Tongue
- English
- Weight
- 657 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0141-5492
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract The demand for recombinant proteins for medical and industrial use is expanding rapidly and plants are now recognized as an efficient, inexpensive means of production. Although the accumulation of recombinant proteins in transgenic plants can be low, we have previously demonstrated that
## Abstract A multiple vector system for the intracellular highβlevel production of affinity tagged recombinant proteins in __Bacillus megaterium__ was developed. The Nβ and Cβterminal fusion of a protein of interest to a Strep II and a His~6~βtag is possible. Corresponding genes are expressed unde
Covalently immobilized biotin was used as a biospecific adsorbant to investigate the application of streptavidin as an affinity domain for simultaneous purification and immobilization of recombinant proteins. A streptavidinp-galactosidase fusion protein was constructed and tested as a model system.