Murphy, G. and Houbrechts, A. and Cockett, M.I. and Williamson, R.A. and O'Shea, M. and Docherty, A.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 .
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.
|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|
|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:||04 May 2012 14:31|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/5311 (The current URI for this page, for reference purposes)|
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