Isolation and characterization of tissue inhibitors of metalloproteinases (TIMP‐1 and TIMP‐2) from human rheumatoid synovial fluid

FEBS Letters

Oberhoff, Renate¹  Tschesche, Harald¹  Osthues, Anja¹  Reinke, Heinz¹  Knäuper, Vera¹ 

[1] University of Beilefeld, Faculty of Chemistry, Department of Biochemistry, P.O. Box 8640, W-4800 Bielefeld I, Germany

关键词: Tissue inhibitor of metalloproteinase;    Gelatinase;    Rheumatoid synovial fluid;   

DOI  :  10.1016/0014-5793(92)80393-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown