Purification and Characterization of BmooAi: A New Toxin from Bothrops moojeni Snake Venom That Inhibits Platelet Aggregation
| Autor: | Rodrigo Simões-Silva, Fábio Luiz de Oliveira, Déborah Fernanda da Cunha Pereira, Carla Cristine Neves Mamede, Thaís M. Migliorini, Kelly Cortes Fonseca, Andreimar M. Soares, Mayara Ribeiro de Queiroz, Leonilda Stanziola, Leonardo A. Calderon, Nadia Cristina Gomes de Morais, Bruna Barbosa de Sousa |
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| Jazyk: | angličtina |
| Rok vydání: | 2014 |
| Předmět: |
Article Subject
Epinephrine Platelet Aggregation Molecular Sequence Data lcsh:Medicine General Biochemistry Genetics and Molecular Biology Bothrops moojeni chemistry.chemical_compound Crotalid Venoms Animals Humans Bothrops Amino Acid Sequence Ristocetin General Immunology and Microbiology Molecular mass biology Edman degradation Chemistry lcsh:R General Medicine biology.organism_classification Chromatography Ion Exchange Molecular Weight Biochemistry Sephadex Snake venom Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Platelet aggregation inhibitor Cattle Collagen Platelet Aggregation Inhibitors Research Article |
| Zdroj: | BioMed Research International BioMed Research International, Vol 2014 (2014) |
| ISSN: | 2314-6141 2314-6133 |
| Popis: | In this paper, we describe the purification/characterization of BmooAi, a new toxin fromBothrops moojenithat inhibits platelet aggregation. The purification of BmooAi was carried out through three chromatographic steps (ion-exchange on a DEAE-Sephacel column, molecular exclusion on a Sephadex G-75 column, and reverse-phase HPLC chromatography on a C2/C18 column). BmooAi was homogeneous by SDS-PAGE and shown to be a single-chain protein of 15,000 Da. BmooAi was analysed by MALDI-TOF Spectrometry and revealed two major components with molecular masses 7824.4 and 7409.2 as well as a trace of protein with a molecular mass of 15,237.4 Da. Sequencing of BmooAi by Edman degradation showed two amino acid sequences: IRDFDPLTNAPENTA and ETEEGAEEGTQ, which revealed no homology to any known toxin from snake venom. BmooAi showed a rather specific inhibitory effect on platelet aggregation induced by collagen, adenosine diphosphate, or epinephrine in human platelet-rich plasma in a dose-dependent manner, whereas it had little or no effect on platelet aggregation induced by ristocetin. The effect on platelet aggregation induced by BmooAi remained active even when heated to 100°C. BmooAi could be of medical interest as a new tool for the development of novel therapeutic agents for the prevention and treatment of thrombotic disorders. |
| Databáze: | OpenAIRE |
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