Mollusc-specific toxins from the venom of Conus textile neovicarius.

Three peptide toxins exhibiting strong paralytic activity to molluscs, but with no paralytic effects on arthropods or vertebrates, were purified from the venom of the molluscivorous snail Conus textile neovicarius from the Red Sea. The amino acid sequences of these mollusc specific toxins are: TxIA, WCKQSGEMCNLLDQNCCDGYCI-VLVCT (identical to the so called 'King Kong peptide'); TxIB, WCKQSGEMCNVLDQNCCDGYCIVFVCT; TxIIA, WGGYSTYC gamma VDS gamma CCSDNCVRSYCT (gamma = gamma-carboxyglutamate). There is a similarity of the Cys framework of these toxins to that of the omega-conotoxins; however, their net negative charges, high content of hydrophobic residues and uneven number of Cys residues in TxIIA, are highly unusual for conotoxins. When assayed on isolated cultured Aplysia neurons, all three toxins induced membrane depolarization and spontaneous repetitive firing. The TxI toxins also induce a marked prolongation of the action potential duration, which is sodium dependent. These effects differ significantly from the blocking activities of piscivorous venom conotoxins. These mollusc specific conotoxins may therefore serve as new and selective probes for ion-channel functions in molluscan neuronal systems.     

Preparation and characterization of a stable half met derivative of type 2 depleted Rhus laccase: Exogenous ligand binding to the type 3 site

We report the preparation and characterization of a stable half met (Cu(II)Cu(I)) type 2 copper depleted derivative of $\text{Rhus}$ laccase. Anion binding studies to this mixed valent type 3 protein form indicate no tight binding of anions nor group 1 - group 2 ligand behavior. This suggests that, in contrast to the well-characterized hemocyanins and tyrosinase coupled binuclear sites, exogenous ligands do $\text{not}$ appear to bridge the type 3 binuclear copper ions in laccase.     

Depolarization exposes the voltage sensor of the sodium channels to the extracellular region

Summary Two domains of Na channels were mapped with site-specific antibodies raised in rabbit against synthetic peptides corresponding to a part of the voltage sensor of internal repeat 1C ₁ ⁺ (amino acids 210–223) and to a region designated dipole (amino acids 1690–1699) of eel electroplax sodium channels. The antibodies bind to their respective domains in both purified and membrane-bound channels and immunoprecipitate the channels from eel electroplax and rat brain synaptosomes.Anti-C ₁ ⁺ depresses the action potential of rat sciatic nerve in a concentration-dependent way. It binds to the external side of rat brain synaptosomal vesicle, and its binding is potentiated by depolarization. Anti-dipole binds to the inner side of the vesicle, and the binding is inhibited by depolarization.We are most grateful to Dr. M.T. Tosteson (Harvard Medical School) for providing us with samples of the S₄IV peptides. We wish to express our gratitude to Drs. D. Gordon (Hebrew University) and A. Safran (The Weizmann Institute) for helping in the immunoprecipitation procedure, to Drs. H. Rahamimoff (Hebrew University) and A. Barzilai (Columbia University) for advising us with the vesicle experiments, to Drs. D. Kassel and M. Gavish (Technion) for many fruitful discussions, and to Dr. Y. Palti (Technion) for discussions of electric field and suggesting the dipole peptide. This work was supported by a basic research fund (BRF) of The Israel Academy of Sciences #430.87 (H.M. and G.S.), a BSF Grant #84-00367 (H.M.) and The Henry Gutwirt Fund for the Promotion of Research-Technion VPR Fund #184-0093 (H.M.).