The recombinant catalytic domain of human neutrophil collagenase lacks type I collagen substrate specificity

Schnierer, S., Kleine, T., Gote, T., Hillemann, A., Knauper, V. ORCID: https://orcid.org/0000-0002-3965-9924 and Tschesche, H. 1993. The recombinant catalytic domain of human neutrophil collagenase lacks type I collagen substrate specificity. Biochemical and Biophysical Research Communications 191 (2) , pp. 319-326. 10.1006/bbrc.1993.1220

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Abstract

The coding region for human neutrophil short form procollagenase lacking the hemopexin like domain coding region was amplified by polymerase chain reaction. Recombinant short form procollagenase was expressed in E.coli and purified in a three step procedure. Renaturation of this proenzyme was carried out by an effective new method using Q-Sepharose chromatography. Treatment of short form procollagenase with mercurials resulted in active short form collagenase Mr 21000 and an intermediate product of Mr 23000. These two products were separated by hydroxamate affinity chromatography. The active, short form collagenase Mr 21000 is stable. Despite full proteolytic activity, it lacks type I collagen substrate specificity and forms the basis for crystallisation experiments.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Dentistry
Publisher:	Elsevier
ISSN:	0006-291X
Last Modified:	31 Aug 2023 12:00
URI:	https://orca.cardiff.ac.uk/id/eprint/161635

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