Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP)

Williamson, Richard A. and Marston, Fiona A. and Angal, Sarojani and Koklitis, P. and Panico, M. and Morris, Howard R. and Carne, A.F. and Smith, B.J. and Harris, T.J. and Freedman, Robert B. (1990) Disulphide bond assignment in human tissue inhibitor of metalloproteinases (TIMP). Biochemical Journal, 268 (2). pp. 267-274. ISSN 0264-6021 . (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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Disulphide bonds in human recombinant tissue inhibitor of metalloproteinases (TIMP) were assigned by resolving proteolytic digests of TIMP on reverse-phase h.p.l.c. and sequencing those peaks judged to contain disulphide bonds by virtue of a change in retention time on reduction. This procedure allowed the direct assignment of Cys-145-Cys-166 and the isolation of two other peptides containing two disulphide bonds each. Further peptide cleavage in conjunction with fast-atom-bombardment m.s. analysis permitted the assignments Cys-1-Cys-70, Cys-3-Cys-99, Cys-13-Cys-124 and Cys-127-Cys-174 from these peptides. The sixth bond Cys-132-Cys-137 was assigned by inference, as the native protein has no detectable free thiol groups.

Item Type: Article
Additional information: 0264-6021 (Print) Journal Article
Uncontrolled keywords: Amino Acid Sequence Animals Cell Line Chromatography, High Pressure Liquid DNA/analysis Disulfides/*analysis *Glycoproteins Humans Hydrolysis Metalloendopeptidases Mice *Microbial Collagenase/antagonists & inhibitors Molecular Sequence Data Pepsin A Recombinant Proteins/genetics Tissue Inhibitor of Metalloproteinases Trypsin
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 09:24
Last Modified: 13 Jun 2014 13:45
Resource URI: https://kar.kent.ac.uk/id/eprint/5321 (The current URI for this page, for reference purposes)
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