Williamson, Richard A., Smith, Bryan J., Angal, Sarojani, Murphy, Gillian, Freedman, Robert B. (1993) Structural analysis of tissue inhibitor of metalloproteinases-1 (TIMP-1) by tryptic peptide mapping. Biochimica Et Biophysica Acta, 1164 (1). pp. 8-16. ISSN 0006-3002. (doi:10.1016/0167-4838(93)90105-z) (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) (KAR id:20742)
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. | |
Official URL: https://doi.org/10.1016/0167-4838(93)90105-z |
Abstract
Tryptic digests of recombinant TIMP-1 have been resolved on reverse-phase HPLC and the major peaks identified by N-terminal sequencing. This procedure accounted for the entire molecule, except two short peptides of 2 and 4 amino acids in length. The peptide map was used to (i), characterize an insoluble 'core' peptide seen on digestion of TIMP-1 in non-reducing conditions; (ii). confirm the structure of DELTA127-184TIMP-1, a recently described truncated form of the TIMP-1 molecule; (iii), identify exposed regions of the intact and truncated TIMP-1 molecules by measuring the rate of tryptic peptide release and (iv), locate sites of aberrant proteolysis seen when recombinant human TIMP-1 was purified at large scale.
Item Type: | Article |
---|---|
DOI/Identification number: | 10.1016/0167-4838(93)90105-z |
Uncontrolled keywords: | tissue inhibitor; proteinase inhibitor; metalloproteinase; peptide mapping; proteolysis |
Subjects: |
Q Science > QP Physiology (Living systems) > QP517 Biochemistry Q Science > QP Physiology (Living systems) > QP506 Molecular biology |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | O.O. Odanye |
Date Deposited: | 13 Jul 2009 18:16 UTC |
Last Modified: | 05 Nov 2024 09:58 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/20742 (The current URI for this page, for reference purposes) |
- Export to:
- RefWorks
- EPrints3 XML
- BibTeX
- CSV
- Depositors only (login required):