An analysis of two refolding routes for a C-terminally truncated human collagenase-3 expressed in Escherichia coli

Hardern, Ian M., Knauper, Vera ORCID: https://orcid.org/0000-0002-3965-9924, Ernill, Richard J., Taylor, Ian W.F., Cooper, Katy L. and Abbott, W.Mark 2000. An analysis of two refolding routes for a C-terminally truncated human collagenase-3 expressed in Escherichia coli. Protein Expression and Purification 19 (2) , pp. 246-252. 10.1006/prep.2000.1244

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Abstract

We describe here the expression of a C-terminally truncated form of human procollagenase-3 in Escherichia coli. The protein was found almost exclusively in inclusion bodies that were solubilized and refolded by two separate methods and then purified on Ni–NTA agarose. The purified proenzyme could be activated with either trypsin or APMA and active enzyme could be purified on a peptidic hydroxamate affinity column. Competitive elution from the affinity matrix yielded a highly purified preparation.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Dentistry
Publisher:	Elsevier
ISSN:	1046-5928
Last Modified:	14 Sep 2023 12:15
URI:	https://orca.cardiff.ac.uk/id/eprint/161600

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