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Comparative studies on three rattlesnake toxins.

S D Aird, I I Kaiser

    Toxicon : Official Journal of the International Society on Toxinology
    |January 1, 1985
    PubMed
    Summary

    The principal toxins from three Crotalus snake venoms are homologous, showing similar structures and functions. Recombining their subunits created hybrid toxins with predictable properties and toxicity.

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    Area of Science:

    • Biochemistry
    • Toxicology
    • Herpetology

    Background:

    • Crotalus snake venoms contain complex toxins.
    • Understanding toxin homology is crucial for antivenom development.

    Purpose of the Study:

    • To compare toxins from Crotalus durissus terrificus, Crotalus s. scutulatus, and Crotalus viridis concolor.
    • To investigate the structural and functional homology of these toxins.

    Main Methods:

    • Gel filtration
    • Ion-exchange chromatography on DEAE-Sephacel
    • Polyacrylamide gel electrophoresis (PAGE) under denaturing and non-denaturing conditions

    Main Results:

    • Native toxins exhibited similar behavior across separation techniques.
    • Subunit dissociation occurred in urea, and recombination restored native toxin properties.
    • Hybrid toxins formed with distinct mobilities, influenced by basic subunits.
    • All native toxins showed comparable LD50 values in mice.
    • Phospholipase activity resides in the basic subunit, with intact toxins showing a lag.

    Conclusions:

    • The principal toxins from these three Crotalus species are homologous.
    • Subunit composition dictates toxin properties and function.
    • Structural homology suggests shared evolutionary origins and potential for cross-neutralization.

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