The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity

Murphy, Gillian and Houbrechts, Annick and Cockett, Mark I. and Williamson, Richard A. and O'Shea, Mark and Docherty, Andrew J. P. (1991) The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity. Biochemistry, 30 (33). pp. 8097-8102. ISSN 0006-2960 . (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1021/bi00247a001

Abstract

Recombinant tissue inhibitor of metalloproteinases (TIMP-1) and a truncated version containing only the three N-terminal loops, delta 127-184TIMP, have been expressed in myeloma cells and purified by affinity chromatography and gel filtration. delta 127-184TIMP was found to exist as two main glycosylation variants of molecular mass 24 kD and 19.5 kDa and an unglycosylated form of 13 kDa. All forms of the truncated inhibitor were able to inhibit and form complexes with active forms of the matrix metalloproteinases, indicating that the major structural features for specific interaction with these enzymes resides in these three loops. Stable binding of delta 127-184TIMP to pro 95-kDa gelatinase was not demonstrable under the conditions for binding of full-length TIMP-1.

Item Type: Article
Additional information: 0006-2960 (Print) Comparative Study Journal Article Research Support, Non-U.S. Gov't
Uncontrolled keywords: Amino Acid Sequence Animals Base Sequence Electrophoresis, Polyacrylamide Gel Enzyme Stability Glycoproteins/*chemistry/genetics/isolation & purification Humans Macromolecular Substances Metalloendopeptidases/*antagonists & inhibitors Mice Molecular Sequence Data Plasmacytoma Rabbits Recombinant Proteins/genetics Tissue Inhibitor of Metalloproteinases Tumor Cells, Cultured
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group
Depositing User: Richard Williamson
Date Deposited: 03 Oct 2009 08:42
Last Modified: 02 Jun 2014 13:50
Resource URI: http://kar.kent.ac.uk/id/eprint/5311 (The current URI for this page, for reference purposes)
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