Purification and characterization of myotoxin IV, a phospholipase A2 variant, from Bothrops asper snake venom

A basic myotoxic protein was purified from Bothrops asper venom. Like other basic Bothrops myotoxins, myotoxin IV induces acute muscle damage after intramuscular injection in mice and disrupts negatively charged liposomes but not positively charged ones. Furthermore, this protein exerts a weak antic...

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Detalhes bibliográficos
Autores: Díaz Oreiro, Cecilia, Lomonte, Bruno, Zamudio, Fernando, Gutiérrez, José María
Formato: artículo
Fecha de publicación:1995
País:Costa Rica
Recursos:Universidad de Costa Rica
Repositorio:Kérwá
OAI Identifier:oai:kerwa.ucr.ac.cr:10669/73297
Acesso em linha:http://onlinelibrary.wiley.com/doi/10.1002/nt.2620030107/full
https://hdl.handle.net/10669/73297
Access Level:acceso embargado
Palavra-chave:Snake venom
Myotoxin
Phospholipases A2
Lys-49 variant
Myonecrosis
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dc.title.es_ES.fl_str_mv Purification and characterization of myotoxin IV, a phospholipase A2 variant, from Bothrops asper snake venom
title Purification and characterization of myotoxin IV, a phospholipase A2 variant, from Bothrops asper snake venom
spellingShingle Purification and characterization of myotoxin IV, a phospholipase A2 variant, from Bothrops asper snake venom
Díaz Oreiro, Cecilia
Snake venom
Myotoxin
Phospholipases A2
Lys-49 variant
Myonecrosis
title_short Purification and characterization of myotoxin IV, a phospholipase A2 variant, from Bothrops asper snake venom
title_full Purification and characterization of myotoxin IV, a phospholipase A2 variant, from Bothrops asper snake venom
title_fullStr Purification and characterization of myotoxin IV, a phospholipase A2 variant, from Bothrops asper snake venom
title_full_unstemmed Purification and characterization of myotoxin IV, a phospholipase A2 variant, from Bothrops asper snake venom
title_sort Purification and characterization of myotoxin IV, a phospholipase A2 variant, from Bothrops asper snake venom
dc.creator.none.fl_str_mv Díaz Oreiro, Cecilia
Lomonte, Bruno
Zamudio, Fernando
Gutiérrez, José María
author Díaz Oreiro, Cecilia
author_facet Díaz Oreiro, Cecilia
Lomonte, Bruno
Zamudio, Fernando
Gutiérrez, José María
author_role author
author2 Lomonte, Bruno
Zamudio, Fernando
Gutiérrez, José María
author2_role author
author
author
dc.subject.es_ES.fl_str_mv Snake venom
Myotoxin
Phospholipases A2
Lys-49 variant
Myonecrosis
topic Snake venom
Myotoxin
Phospholipases A2
Lys-49 variant
Myonecrosis
description A basic myotoxic protein was purified from Bothrops asper venom. Like other basic Bothrops myotoxins, myotoxin IV induces acute muscle damage after intramuscular injection in mice and disrupts negatively charged liposomes but not positively charged ones. Furthermore, this protein exerts a weak anticoagulant effect only at concentrations of 40 μg/ml or higher, and is devoid of phospholipase A2 activity. Rabbit polyclonal antibodies to B. asper myotoxin II, a related lysine-49 isoform, cross-react strongly with myotoxin IV by enzyme immunoassay, indicating a high degree of antigenic similarity between these two proteins. The fact that both toxins have similar amino acid compositions and amino-terminal sequences, including leucine-5 and glutamine-11, 2 amino acid residues conserved in all lysine-49 phospholipase A2 variants purified, strongly suggests that B. asper myotoxin IV is a lysine-49 phospholipase A2.
publishDate 1995
dc.date.issued.none.fl_str_mv 1995
dc.date.accessioned.none.fl_str_mv 2017-09-26T20:12:53Z
dc.date.available.none.fl_str_mv 2017-09-26T20:12:53Z
dc.type.none.fl_str_mv artículo original
http://purl.org/coar/resource_type/c_2df8fbb1
info:eu-repo/semantics/article
format article
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dc.identifier.issn.none.fl_str_mv 1522-7189
dc.identifier.uri.none.fl_str_mv https://hdl.handle.net/10669/73297
dc.identifier.doi.none.fl_str_mv 10.1002/nt.2620030107
dc.identifier.pmid.none.fl_str_mv 7749580
url http://onlinelibrary.wiley.com/doi/10.1002/nt.2620030107/full
https://hdl.handle.net/10669/73297
identifier_str_mv 1522-7189
10.1002/nt.2620030107
7749580
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dc.rights.none.fl_str_mv acceso embargado
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info:eu-repo/semantics/embargoedAccess
rights_invalid_str_mv acceso embargado
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eu_rights_str_mv embargoedAccess
dc.source.es_ES.fl_str_mv Natural Toxins, Vol. 3, Núm. 1, 1995
dc.source.none.fl_str_mv reponame:Kérwá
instname:Universidad de Costa Rica
instacron:UCR
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spelling Díaz Oreiro, Ceciliaf49daa4d-080c-4cf2-9856-a48ede706fba600Lomonte, Bruno581484ad-aaa8-46b1-bc0e-f380d895640c600Zamudio, Fernando021d189f-101c-4914-b325-23f2005d9d42Gutiérrez, José María6a9bac5f-130f-4977-8ddf-ab97fcafacc46002017-09-26T20:12:53Z2017-09-26T20:12:53Z1995http://onlinelibrary.wiley.com/doi/10.1002/nt.2620030107/full1522-7189https://hdl.handle.net/10669/7329710.1002/nt.26200301077749580A basic myotoxic protein was purified from Bothrops asper venom. Like other basic Bothrops myotoxins, myotoxin IV induces acute muscle damage after intramuscular injection in mice and disrupts negatively charged liposomes but not positively charged ones. Furthermore, this protein exerts a weak anticoagulant effect only at concentrations of 40 μg/ml or higher, and is devoid of phospholipase A2 activity. Rabbit polyclonal antibodies to B. asper myotoxin II, a related lysine-49 isoform, cross-react strongly with myotoxin IV by enzyme immunoassay, indicating a high degree of antigenic similarity between these two proteins. The fact that both toxins have similar amino acid compositions and amino-terminal sequences, including leucine-5 and glutamine-11, 2 amino acid residues conserved in all lysine-49 phospholipase A2 variants purified, strongly suggests that B. asper myotoxin IV is a lysine-49 phospholipase A2.Universidad de Costa Rica/[Project 741-90-044]/UCR/Costa RicaUCR::Vicerrectoría de Investigación::Unidades de Investigación::Ciencias de la Salud::Instituto Clodomiro Picado (ICP)UCR::Vicerrectoría de Docencia::Salud::Facultad de Microbiologíaen_USacceso embargadohttp://purl.org/coar/access_right/c_f1cfinfo:eu-repo/semantics/embargoedAccessNatural Toxins, Vol. 3, Núm. 1, 1995reponame:Kérwáinstname:Universidad de Costa Ricainstacron:UCRSnake venomMyotoxinPhospholipases A2Lys-49 variantMyonecrosisPurification and characterization of myotoxin IV, a phospholipase A2 variant, from Bothrops asper snake venomartículo originalhttp://purl.org/coar/resource_type/c_2df8fbb1info:eu-repo/semantics/articleORIGINAL1995_PLA2_NatToxins_Diaz_myotoxin_IV.pdf1995_PLA2_NatToxins_Diaz_myotoxin_IV.pdfapplication/pdf673071https://www.kerwa.ucr.ac.cr/bitstreams/2b6ce8c0-2df3-4a61-93e5-9a00797f72f7/download6636efa78910c0714352dd7d81d163a0MD51TEXT1995_PLA2_NatToxins_Diaz_myotoxin_IV.pdf.txt1995_PLA2_NatToxins_Diaz_myotoxin_IV.pdf.txtExtracted texttext/plain6https://www.kerwa.ucr.ac.cr/bitstreams/076832d4-d516-4e30-b44b-64d10bae91b0/download6d93d3216dc4a7f5df47d4876fbec4d3MD54THUMBNAIL1995_PLA2_NatToxins_Diaz_myotoxin_IV.pdf.jpg1995_PLA2_NatToxins_Diaz_myotoxin_IV.pdf.jpgGenerated Thumbnailimage/jpeg6559https://www.kerwa.ucr.ac.cr/bitstreams/9bb31470-db88-46e7-9412-08f39eefd3d0/download11ddc98e348ed7eab134518eb0e24128MD55LICENSElicense.txtlicense.txttext/plain; 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