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At least 109 records · Page 6Linked to original sources
PubMed1992

Hemorrhagic, fibrinogenolytic and edema-forming activities of the venom of the colubrid snake Philodryas olfersii (green snake).

The venom of P. olfersii has high hemorrhagic, edema-inducing and fibrin(ogen)olytic activities. It is devoid of thrombin-like, procoagulant, phospholipase A2 and platelet aggregating enzymes. The main activities are metalloproteinases inhibited by metal chelators (EDTA and 1,10-phenanthroline) and sulfhydryl compounds (DTT and cysteine). The hemorrhagic and fibrinogenolytic enzymes were partially purified by gel filtration on HPLC. The hemorrhagic activity of the venom was neutralized by commercial horse antivenoms to Bothrops species, as well as by rabbit antisera specific for hemorrhagic factors isolated from these Bothrops venoms. No immunoprecipitin reactions were obtained, indicating that the few epitopes of the P. olfersii hemorrhagin are involved in these neutralization reactions. The fibrinogenolytic enzyme cleaves A alpha-chain more quickly than the B beta-chain of human fibrinogen. The venom also solubilizes fibrin. This solubilization appears to occur from the hydrolysis of unpolymerized alpha-chain and cross-linked gamma-gamma dimer. The fibrin peptide products are distinct from those produced by plasmin.

Animals↗
PubMed1983

Protective effect of snake venom antibodies in sera of previous snake bite victims.

Three out of seven serum samples from Ecuadorian Indians had very high antibody levels against Bothrops nasutus venom, and IgG concentrates of these sera effectively neutralized this venom when subsequently injected into mice. It is concluded that the high mortality rate among these Indians would be even higher if there were not such natural protection. Further research into active immunization of humans should be encouraged.

Animals↗
PubMed1999

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).

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.

Animals↗