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Protein C activators in snake venoms.

K Stocker, H Fischer, J Meier

    Behring Institute Mitteilungen
    |February 1, 1986
    PubMed
    Summary

    Snake venoms contain protein C (PC) activators. A specific activator, Protac from Agkistrodon contortrix contortrix, is stable and useful for quantitative PC determination, showing no acute toxicity in rabbits.

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    Area of Science:

    • Biochemistry
    • Toxicology
    • Pharmacology

    Background:

    • Snake venoms are complex biological mixtures.
    • Protein C (PC) is a crucial anticoagulant protein.
    • Identifying PC activators in venoms is important for biochemical research.

    Purpose of the Study:

    • To screen snake venoms for protein C (PC) activating potency.
    • To characterize a stable PC activator from Agkistrodon contortrix contortrix venom.
    • To evaluate the potential of this activator for quantitative PC determination.

    Main Methods:

    • Chromogenic substrate assay for amidolytic activity.
    • Testing PC activating potency in venoms from 32 snake species.
    • Heat stability assays at 70°C, pH 3 for 10 minutes.
    • Purification and characterization of the PC activator (Protac).
    • In vivo studies in rabbits to assess toxicity and effects on APTT.

    Main Results:

    • Eleven out of 32 snake venoms showed PC activating potency.
    • PC activators from five venoms were heat-labile, while six were heat-stable.
    • Protac, purified from A. c. contortrix venom, is a 39-42 kDa polypeptide.
    • Protac lacks proteinase activity, is inhibitor-resistant, and acts stoichiometrically.
    • Protac prolonged APTT in rabbits without causing acute toxicity.

    Conclusions:

    • Snake venoms are a source of diverse protein C activators.
    • Protac is a heat-stable, non-proteolytic PC activator with potential for quantitative assays.
    • Protac offers advantages over thrombin for protein C determination and appears safe in vivo.

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