Osthues, Anja, Knauper, Vera ![]() |
Abstract
The tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2 were purified to apparent homogeneity from human rheumatoid synovial fluid (HRSF). The inhibitors were isolated by dissociation of non-covalent gelatinase/TIMP complexes. TIMP-1 migrated as a single polypeptide with M r 28 500 on SDS-PAGE, while the M r of TIMP-2 was 21 000. The inhibitory activity was stable under heat and acid pH. N-terminal sequence data were obtained for the first 15 residues of both inhibitors and showed identity to the human fibroblast inhibitors TIMP-1 and TIMP-2. This is the first demonstration that TIMP-1 and TIMP-2 can be directly purified from human rheumatoid synovial fluid. The complex formation between the metalloproteinase inhibitors and leucocyte metalloproteinases was shown by immunoblotting.
Item Type: | Article |
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Date Type: | Publication |
Status: | Published |
Schools: | Schools > Dentistry |
Publisher: | Federation of European Biochemical Societies |
ISSN: | 1873-3468 |
Last Modified: | 31 Aug 2023 15:15 |
URI: | https://orca.cardiff.ac.uk/id/eprint/161629 |
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