|
|||||
|
|
The complete amino acid sequence of toxin TsTX-VI isolated from the venom of the scorpionTityus serrulatus |
|
| Authors: | Sergio Marangoni Jorge Ghiso Suely V. Sampaio Eliane C. Arantes José R. Giglio Benedito Oliveira Blas Frangione |
| Affiliation: | 1. Department of Pathology, New York University Medical Center, 550 First Avenue, 10016, New York, New York 3. Departamento de Análises Clínicas, Toxicológicas e Bromatológicas, Faculdade de Ciências Farmacêuticas de Ribeir?o Preto, Universidade de S?o Paulo, 14.049, Ribeir?o Preto—SP, Brasil 4. Departamento de Física e Química, Faculdade de Ciências Farmacêuticas de Ribeir?o Preto, Universidade de S?o Paulo, 14.049, Ribeir?o Preto—SP, Brasil 5. Departamento de Bioquímica, Faculdade de Medicina de Ribeir?o Preto, Universidade de S?o Paulo, 14.049, Ribeir?o Preto—SP, Brasil 2. Departamento de Bioquímica, Instituto de Biologia, Universidade Estadual de Campinas, C.P. 6109, 13081, Campinas—SP, Brasil |
| Abstract: | The complete sequence of the toxin TsTX-VI from the venom of the scorpionTityus serrulatus Lutz and Mello is presented. The sequence has been determined by automated Edman analysis of the reduced and carboxymethylated protein as well as of the resulting peptides, obtained fromS. aureus protease and tryptic digestions. TsTX-VI is composed of 62 residues and has a calculated molecular weight of 6717. Homology studies with other scorpion toxins show that TsTX-VI is more similar to the Old World than to the North American scorpion toxins. The hydropathic index indicates that TsTX-VI is more hydrophobic than Ts-γ. Toxicity studies carried out in mice demonstrate that i.v. injection of TsTX-VI is unable to evoke the usual symptoms induced by the typical neurotoxins of this venom, but only a generalized allergic reaction. These properties are important in clarifying the relationship between primary structure and biological function of scorpion toxins. |
| Keywords: | |
| 本文献已被 SpringerLink 等数据库收录！ | |