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Venom characterization of the Amazonian scorpion Tityus metuendus.
Batista, C V F; Martins, J G; Restano-Cassulini, R; Coronas, F I V; Zamudio, F Z; Procópio, R; Possani, L D.
Afiliação
  • Batista CVF; Laboratorio Universitario de Proteomica, Instituto de Biotecnología, Universidad Nacional Autonoma de Mexico, Avenida Universidad 2001, Apartado Postal 510-3, Cuernavaca, Morelos 62210, Mexico.
  • Martins JG; Pós-Graduação em Biotecnologia e Recursos Naturais, Universidade do Estado do Amazonas - UEA, Avenida Carvalho Leal, nº 1777, Manaus, Amazonas, Brazil.
  • Restano-Cassulini R; Departmento de Medicina Molecular y Bioprocesos, Instituto de Biotecnologia, Universidad Nacional Autónoma de México, Avenida Universidad, 2001, Cuernavaca, Morelos 62210, Mexico.
  • Coronas FIV; Departmento de Medicina Molecular y Bioprocesos, Instituto de Biotecnologia, Universidad Nacional Autónoma de México, Avenida Universidad, 2001, Cuernavaca, Morelos 62210, Mexico.
  • Zamudio FZ; Departmento de Medicina Molecular y Bioprocesos, Instituto de Biotecnologia, Universidad Nacional Autónoma de México, Avenida Universidad, 2001, Cuernavaca, Morelos 62210, Mexico.
  • Procópio R; Pós-Graduação em Biotecnologia e Recursos Naturais, Universidade do Estado do Amazonas - UEA, Avenida Carvalho Leal, nº 1777, Manaus, Amazonas, Brazil.
  • Possani LD; Departmento de Medicina Molecular y Bioprocesos, Instituto de Biotecnologia, Universidad Nacional Autónoma de México, Avenida Universidad, 2001, Cuernavaca, Morelos 62210, Mexico. Electronic address: possani@ibt.unam.mx.
Toxicon ; 143: 51-58, 2018 Mar 01.
Article em En | MEDLINE | ID: mdl-29337221
ABSTRACT
The soluble venom from the scorpion Tityus metuendus was characterized by various methods. In vivo experiments with mice showed that it is lethal. Extended electrophysiological recordings using seven sub-types of human voltage gated sodium channels (hNav1.1 to 1.7) showed that it contains both α- and ß-scorpion toxin types. Fingerprint analysis by mass spectrometry identified over 200 distinct molecular mass components. At least 60 sub-fractions were recovered from HPLC separation. Five purified peptides were sequenced by Edman degradation, and their complete primary structures were determined. Additionally, three other peptides have had their N-terminal amino acid sequences determined by Edman degradation and reported. Mass spectrometry analysis of tryptic digestion of the soluble venom permitted the identification of the amino acid sequence of 111 different peptides. Search for similarities of the sequences found indicated that they probably are sodium and potassium channel toxins, metalloproteinases, hyaluronidases, endothelin and angiotensin-converting enzymes, bradykinin-potentiating peptide, hypothetical proteins, allergens, other enzymes, other proteins and peptides.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Venenos de Escorpião / Escorpiões Tipo de estudo: Prognostic_studies Limite: Animals / Female / Humans / Male Idioma: En Revista: Toxicon Ano de publicação: 2018 Tipo de documento: Article País de afiliação: México

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Venenos de Escorpião / Escorpiões Tipo de estudo: Prognostic_studies Limite: Animals / Female / Humans / Male Idioma: En Revista: Toxicon Ano de publicação: 2018 Tipo de documento: Article País de afiliação: México