Williamson, Richard A. (2010) Refolding of TIMP-2 from Escherichia coli Inclusion Bodies. Refolding of TIMP-2 from Escherichia coli Inclusion Bodies, 622 . pp. 111-121. ISSN 1064-3745.
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| Official URL http://dx.doi.org/10.1007/978-1-60327-299-5_7 |
Abstract
The TIMP proteins contain six intramolecular disulfide bonds and form unfolded insoluble aggregates when expressed in E. coli. Eukaryotic expression systems provide the necessary post-translational modification apparatus to produce authentic TIMP but are comparatively slow and more expensive. This chapter describes the production of native TIMP-2 (both full-length and the N-terminal domain) from E. coli by in vitro refolding. The technique allows high-level intracellular expression and efficient isolation of the recombinant product without the use of fusion tags or partners. Protein purity after ion exchange and gel filtration chromatography was judged to be greater than 95% with yields of 15 mg/L from LB medium and 10 mg/L from minimal medium.
| Item Type: | Article |
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| Additional information: | Also published in Methods in Molecular Biology Vol. 151, 2001. See KAR ID 5317. |
| Subjects: | Q Science |
| Divisions: | Faculties > Science Technology and Medical Studies > School of Biosciences |
| Depositing User: | Sue Davies |
| Date Deposited: | 09 Oct 2012 13:08 |
| Last Modified: | 04 Feb 2013 10:32 |
| Resource URI: | http://kar.kent.ac.uk/id/eprint/31440 (The current URI for this page, for reference purposes) |
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