Biochemical characteristics of fibrolase, a fibrinolytic protease from snake venom.

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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
DrugTargetKindOrganismPharmacological ActionActions
AlfimepraseFibrinogen alpha chainProteinHumans
Unknown
Not AvailableDetails
AlfimepraseFibrinogen beta chainProteinHumans
Unknown
Not AvailableDetails