Kinetics of association of human proteinases with human alpha 2-macroglobulin
| Autor: | J Travis, G D Virca |
|---|---|
| Rok vydání: | 1984 |
| Předmět: |
Cathepsin
Elastase Alpha (ethology) Cell Biology Kallikrein Biology Cathepsin G Biochemistry Molecular biology alpha-2-Macroglobulin chemistry.chemical_compound chemistry immune system diseases Neutrophil elastase biology.protein Molecular Biology Pancreatic elastase circulatory and respiratory physiology |
| Zdroj: | Journal of Biological Chemistry. 259:8870-8874 |
| ISSN: | 0021-9258 |
| DOI: | 10.1016/s0021-9258(17)47234-6 |
| Popis: | Association rates have been determined for the interaction of human alpha 2-macroglobulin with human neutrophil elastase, cathepsin G, and human plasma kallikrein. Both of the neutrophil enzymes are rapidly inactivated by this inhibitor; however, the inactivation of plasma kallikrein is much slower. Comparison of the rates of inactivation with those already established for other inhibitors clearly indicate that alpha 1-proteinase inhibitor is the controlling inhibitor for neutrophil elastase and alpha 1-antichymotrypsin for cathepsin G, alpha 2-macroglobulin acting only as a secondary inhibitor. The control of plasma kallikrein would appear to be rather poor since neither alpha 2-macroglobulin nor C1-inhibitor appears to react very rapidly with this proteinase. Thus, a primary role for alpha 2-macroglobulin in directly inactivating proteinases in blood, under normal physiological conditions, remains to be established. |
| Databáze: | OpenAIRE |
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