| Autor: |
Swenson, S., Markland, F. S. |
| Předmět: |
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| Zdroj: |
Toxin Reviews; 2006, Vol. 25 Issue 4, p351-378, 28p, 4 Diagrams, 5 Charts, 2 Graphs |
| Abstrakt: |
Snake venoms contain a number of serine and metalloproteinases, included among these are the fibrinolytic metalloproteinases. When the fibrinolytic enzymes were first isolated from viper venoms, it was postulated that there may be a clinical application for these enzymes. In the ensuing years, a substantial body of literature has been generated on the identification and characterization of the fibrinolytic enzymes from a broad spectrum of snake species. In this report, we describe the biological properties and features of the enzyme known as fibrolase. Fibrolase, a fibrinolytic metalloproteinase, has been isolated from Agkistrodon contortrix contortrix (southern copperhead) venom. The biochemical, structural, and physiochemical properties of the enzyme are described. In addition, in vitro bioactivity studies with a size-altered version of the enzyme and a derivative with altered binding capabilities are described. The size-modified form of fibrolase was formed through the adduction of polyethylene glycol to the native protein in an effort to reduce the rate of clearance from the circulation by α 2-macroglobulin. Alteration in the binding affinity of the enzyme to platelets was achieved through coupling fibrolase to an Arg-Gly-Asp (RGD)-like peptide; this modification imparts an inhibitory activity on platelet aggregation and thrombus formation, while maintaining full fibrinolytic activity. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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