Biochemical characteristics of fibrolase, a fibrinolytic protease from snake venom.
Article Details
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Ahmed NK, Tennant KD, Markland FS, Lacz JP
Biochemical characteristics of fibrolase, a fibrinolytic protease from snake venom.
Haemostasis. 1990;20(3):147-54.
- PubMed ID
- 1696922 [ View in PubMed]
- Abstract
Fibrolase, a fibrinolytic enzyme isolated from Agkistrodon c. contortrix (southern copperhead) venom, solubilizes fibrin primarily by rapid hydrolysis of the alpha and beta chains. Fibrolase is also an A alpha, B beta fibrinogenase. The breakdown products of fibrin and fibrinogen following incubation with fibrolase were different from those observed with plasmin. This enzyme is a metalloprotease that was inhibited by ethylenediaminetetraacetic acid. Fibrolase was inhibited by dithiothreitol, suggesting that disulfide bonds are important for catalytic activity. It was also inhibited by alpha 2-macroglobulin, but not by the soybean or lima bean trypsin inhibitors, diisopropylfluorophosphate, or p-hydroxymercuribenzoate. Unlike thrombolytic agents such as streptokinase, fibrolase does not activate plasminogen as evidenced by the use of plasmin-specific chromogenic substrate S-2251 and by sodium dodecyl sulfate-polyacrylamide gel electrophoresis.
DrugBank Data that Cites this Article
- Drug Targets
Drug Target Kind Organism Pharmacological Action Actions Alfimeprase Fibrinogen alpha chain Protein Humans UnknownNot Available Details Alfimeprase Fibrinogen beta chain Protein Humans UnknownNot Available Details