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Thrombin-like snake venom proteinases

K Stocker, H Fischer, J Meier

    Toxicon : Official Journal of the International Society on Toxinology
    |January 1, 1982
    PubMed
    Summary
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    Snake venom proteinases can alter blood coagulation by affecting fibrinogen. Some enzymes release fibrinopeptide A, leading to afibrinogenemia, while others have varied interactions with inhibitors and human fibrinogen.

    Area of Science:

    • Biochemistry
    • Toxicology
    • Hematology

    Background:

    • Crotalidae and Viperidae snake venoms contain proteinases targeting thrombin substrates.
    • These enzymes exhibit diverse activities, including fibrinogen coagulation, platelet effects, and factor V, VIII, and XIII modification.

    Purpose of the Study:

    • To characterize fibrinogen-altering proteinases from snake venoms.
    • To investigate their mechanisms of action, inhibition, and defibrinogenating potential.

    Main Methods:

    • Isolation and characterization of snake venom proteinases.
    • In vitro assays for fibrinogen coagulation and fibrinopeptide release.
    • Assessment of enzyme inhibition by antithrombin III-heparin and hirudin.
    • In vivo studies on defibrinogenation and venom toxicity.

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    Main Results:

    • Fibrinogen-specific proteinases release fibrinopeptide A, B, or both.
    • Some enzymes are inhibited by AT III-heparin, while others are resistant.
    • Fibrinogen-depleting proteinases cause afibrinogenemia.
    • Batroxobin from B. moojeni is a more effective defibrinogenating agent in humans than from B. atrox.

    Conclusions:

    • Snake venom proteinases display varied mechanisms in altering blood coagulation.
    • Species-specific interactions influence defibrinogenating efficacy.
    • Batroxobin's role in Bothrops venom poisoning appears minor.
    • Understanding these enzymes aids in developing antivenoms and therapeutic agents.