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  • Title: Partial purification of acetylcholine receptor binding components from the Duvernoy's secretions of blanding's tree snake (Boiga blandingi) and the mangrove snake (Boiga dendrophila).
    Author: Broaders M, Faro C, Ryan MF.
    Journal: J Nat Toxins; 1999 Jun; 8(2):155-66. PubMed ID: 10410327.
    Abstract:
    Acetylcholine receptor (AChR) binding activity was detected in Duvernoy's secretions from B. blandingi and B. dendrophila as they competitively inhibited formation of 3[H]bungarotoxin-acetylcholine receptor complexes (3[H]Bgt-AChR) in a concentration-dependent manner. Secretions contained two types of toxin: low affinity and high affinity. Reversed-phase HPLC of B. blandingi and B. dendrophila secretions afforded 20 and 14 peaks, respectively. AChR binding components, as revealed by SDS-PAGE, had apparent molecular weights of 10 and 11 kDa (B. blandingi) or 11 and 12 kDa (B. dendrophila). Periodic acid-Schiff staining indicated these were not glycoproteins. Alkylation with 4-vinylpyridine significantly decreased their ability to inhibit 3[H]Bgt-AChR binding, indicating disulphide bridges were necessary for receptor-binding activity. Attempts to sequence the B. blandingi peptides were negative as these components seemed to be N-terminally blocked.
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