Structural and functional comparison of toxins from the venom of the scorpions Centruroides infamatus infamatus, centruroides limpidus limpidus and Centruroides noxius
| Autor: | Alberto Darszon, A.N. Ramírez, A. Liévano, Manuel Dehesa-Dávila, Lourival D. Possani, Fernando Z. Zamudio, Georgina Gurrola-Briones |
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| Rok vydání: | 1996 |
| Předmět: |
Physiology
Molecular Sequence Data Synaptic Membranes Xenopus Scorpion Venoms Venom Biology medicine.disease_cause Binding Competitive Biochemistry Sodium Channels Scorpions Mice Xenopus laevis Species Specificity medicine Animals Amino Acid Sequence Binding site Muscle Skeletal Molecular Biology Centruroides infamatus Peptide sequence chemistry.chemical_classification Binding Sites Sequence Homology Amino Acid Toxin Brain biology.organism_classification Molecular biology Rats Amino acid chemistry Chromatography Gel Oocytes Centruroides noxius Female Synaptosomes |
| Zdroj: | Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 113:331-339 |
| ISSN: | 1096-4959 |
| DOI: | 10.1016/0305-0491(95)02031-4 |
| Popis: | Two novel toxins containing 66 amino acid residues each were isolated from the venom of the scorpions Centruroides infamatus infamatus and Centruroides limpidus limpidus, respectively. Their full amino acid sequences were determined. Comparison of primary structures showed that they share 97% similarity among themselves and 83% to that of toxin 2 from Centruroides noxius. The three toxins studied compete with each other for the same binding sites on membranes prepared from rat brain synaptosomes, suggesting that they are all beta-scorpion toxins. Toxin action was assayed into the microI-2 rat skeletal muscle Na+ channel heterologously expressed into Xenopus oocytes. All three toxins block this Na+ channel in a similar fashion, without affecting inactivation, and showed IC50 values in the micromolar concentration range. |
| Databáze: | OpenAIRE |
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