BOHM, B and DEUTZMANN, R and BURKHARDT, H (1991) PURIFICATION OF A SERINE-PROTEINASE INHIBITOR FROM HUMAN ARTICULAR-CARTILAGE - IDENTITY WITH THE ACID-STABLE PROTEINASE-INHIBITOR OF MUCOUS SECRETIONS. BIOCHEMICAL JOURNAL, 274. pp. 269-273. ISSN 0264-6021, 1470-8728
Full text not available from this repository.Abstract
An inhibitor of the serine proteinases human leucocyte elastase (EC 3.4.21.37), of cathepsin G (EC 3.4.21.20) and of trypsin (EC 3.4.21.4) has been purified from human articular cartilage. The apparent M(r) of the cationic (pI > 10) protein was determined to 15000 by SDS/PAGE. It was shown to cross-react in Western blot with a specific antibody to a recombinant-derived serine-proteinase inhibitor of human mucous secretions. Identity of both inhibitors is indicated by the determination of the N-terminal amino acid sequence of the cartilage-derived serine-proteinase inhibitor. In all 24 residues the cartilage inhibitor was shown to be identical with the human secretory leucocyte proteinase inhibitor ('SLPI'). The inhibitor molecule may play a crucial role in the protection of cartilage matrix proteins against proteolytic attack.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | METALLOPROTEINASE INHIBITOR; POLYACRYLAMIDE GELS; TISSUE INHIBITOR; CATHEPSIN-G; COLLAGENASE; LEUKOCYTE; SEQUENCE; ANTILEUKOPROTEASE; CHYMOTRYPSIN; SPECIFICITY; |
| Depositing User: | Dr. Gernot Deinzer |
| Last Modified: | 19 Oct 2022 08:46 |
| URI: | https://pred.uni-regensburg.de/id/eprint/55081 |
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