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Defibrinogenation with benzoyl-batroxobin.

F Markwardt, M Paintz, M Richter

    Thrombosis Research
    |October 1, 1985
    PubMed
    Summary

    Acylating batroxobin, a protease from B. moojeni, creates benzoyl-batroxobin. This inactive form, when injected into rats, showed slower defibrinogenation and prevented microthrombosis compared to active batroxobin.

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    Area of Science:

    • Biochemistry
    • Pharmacology
    • Toxicology

    Background:

    • Batroxobin is a serine protease from Bothrops moojeni venom.
    • It exhibits significant thrombin-like and fibrinogen-clotting activity.
    • Understanding its derivatives can reveal insights into protease inhibition and function.

    Purpose of the Study:

    • To investigate the enzymatic inactivation and in vivo effects of acylated batroxobin.
    • To compare the defibrinogenation and thrombotic potential of batroxobin and its derivative, benzoyl-batroxobin.
    • To explore the therapeutic implications of modified snake venom proteases.

    Main Methods:

    • Acylation of batroxobin with 4-amidinophenyl benzoate at the active site serine hydroxyl.
    • Characterization of the enzymatic inactivity and deacylation kinetics of benzoyl-batroxobin.
    • Intravenous administration of batroxobin and benzoyl-batroxobin in rats to assess plasma clotting activity, defibrinogenation, and microthrombosis.

    Main Results:

    • Benzoyl-batroxobin was formed, exhibiting enzymatic inactivity with a deacylation half-life of approximately one hour, restoring clotting activity upon deacylation.
    • In vivo studies showed significantly retarded defibrinogenation with benzoyl-batroxobin compared to batroxobin.
    • Batroxobin induced initial microthrombosis, whereas equivalent doses of benzoyl-batroxobin did not cause this effect.

    Conclusions:

    • Acylation effectively inactivates batroxobin's enzymatic and pro-thrombotic activities.
    • Benzoyl-batroxobin serves as a prodrug, releasing active batroxobin slowly in vivo.
    • This modified protease demonstrates a reduced potential for causing microthrombosis, suggesting potential applications in anticoagulation therapy.

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