Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom
Autor(a) principal: | |
---|---|
Data de Publicação: | 2011 |
Outros Autores: | , , , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNESP |
Texto Completo: | http://dx.doi.org/10.1590/S1678-91992011000100004 http://hdl.handle.net/11449/11651 |
Resumo: | Gyroxin, a thrombin-like enzyme isolated from Crotalus durissus terrificus venom and capable of converting fibrinogen into fibrin, presents coagulant and neurotoxic activities. The aim of the present study was to evaluate such coagulant and toxic properties. Gyroxin was isolated using only two chromatographic steps - namely gel filtration (Sephadex G-75) and affinity (Benzamidine Sepharose 6B) -resulting in a sample of high purity, as evaluated by RP-HPLC C2/C18 and electrophoretic analysis that showed a molecular mass of 30 kDa. Gyroxin hydrolyzed specific chromogenic substrates, which caused it to be classified as a serine proteinase and thrombin-like enzyme. It was stable from pH 5.5 to 8.5 and inhibited by Mn(2)+, Cu(2)+, PMSF and benzamidine. Human plasma coagulation was more efficient at pH 6.0. An in vivo toxicity test showed that only behavioral alterations occurred, with no barrel rotation. Gyroxin was not able to block neuromuscular contraction in vitro, which suggests that its action, at the studied concentrations, has no effect on the peripheral nervous system. |
id |
UNSP_efc0dcff27f12820081459a643b855f9 |
---|---|
oai_identifier_str |
oai:repositorio.unesp.br:11449/11651 |
network_acronym_str |
UNSP |
network_name_str |
Repositório Institucional da UNESP |
repository_id_str |
2946 |
spelling |
Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venomgyroxinneurotoxicitycoagulant activityCrotalus durissus terrificusserine proteinaseGyroxin, a thrombin-like enzyme isolated from Crotalus durissus terrificus venom and capable of converting fibrinogen into fibrin, presents coagulant and neurotoxic activities. The aim of the present study was to evaluate such coagulant and toxic properties. Gyroxin was isolated using only two chromatographic steps - namely gel filtration (Sephadex G-75) and affinity (Benzamidine Sepharose 6B) -resulting in a sample of high purity, as evaluated by RP-HPLC C2/C18 and electrophoretic analysis that showed a molecular mass of 30 kDa. Gyroxin hydrolyzed specific chromogenic substrates, which caused it to be classified as a serine proteinase and thrombin-like enzyme. It was stable from pH 5.5 to 8.5 and inhibited by Mn(2)+, Cu(2)+, PMSF and benzamidine. Human plasma coagulation was more efficient at pH 6.0. An in vivo toxicity test showed that only behavioral alterations occurred, with no barrel rotation. Gyroxin was not able to block neuromuscular contraction in vitro, which suggests that its action, at the studied concentrations, has no effect on the peripheral nervous system.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)UNESP, São Paulo State Univ, CEVAP, BR-18618000 Botucatu, SP, BrazilUNESP, São Paulo State Univ, Botucatu Med Sch, Dept Trop Dis & Imaging Diag, BR-18618000 Botucatu, SP, BrazilUniv São Paulo, Dept Clin Toxicol & Bromatol Anal, Sch Pharmaceut Sci, BR-14049 Ribeirao Preto, SP, BrazilUniversidade Federal de Uberlândia (UFU), Inst Genet & Biochem, BR-38400 Uberlandia, MG, BrazilUniv Fed Fluminense, Inst Biol, Dept Cellular & Mol Biol, Niteroi, RJ, BrazilUniv São Paulo, Med Sch Ribeirao Preto, Dept Biochem & Immunol, Ribeirao Preto, SP, BrazilUNESP, São Paulo State Univ, Inst Biol, Dept Pharmacol, BR-18618000 Botucatu, SP, BrazilUNESP, São Paulo State Univ, Botucatu Med Sch, Dept Dermatol, BR-18618000 Botucatu, SP, BrazilUNESP, São Paulo State Univ, CEVAP, BR-18618000 Botucatu, SP, BrazilUNESP, São Paulo State Univ, Botucatu Med Sch, Dept Trop Dis & Imaging Diag, BR-18618000 Botucatu, SP, BrazilUNESP, São Paulo State Univ, Inst Biol, Dept Pharmacol, BR-18618000 Botucatu, SP, BrazilUNESP, São Paulo State Univ, Botucatu Med Sch, Dept Dermatol, BR-18618000 Botucatu, SP, BrazilFAPESP: 07/05159-7Universidade Estadual Paulista (Unesp), Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP)Universidade Estadual Paulista (Unesp)Universidade de São Paulo (USP)Universidade Federal de Uberlândia (UFU)Universidade Federal Fluminense (UFF)Barros, L. C. [UNESP]Soares, A. M.Costa, F. L.Rodrigues, V. M.Fuly, A. L.Giglio, J. R.Gallacci, Marcia [UNESP]Thomazini-Santos, I. A. [UNESP]Barraviera, Silvia Regina Catharino Sartori [UNESP]Barraviera, Benedito [UNESP]Ferreira Júnior, Rui Seabra [UNESP]2014-05-20T13:34:02Z2014-05-20T13:34:02Z2011-01-01info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/article23-33application/pdfhttp://dx.doi.org/10.1590/S1678-91992011000100004Journal of Venomous Animals and Toxins Including Tropical Diseases. Botucatu: Cevap-unesp, v. 17, n. 1, p. 23-33, 2011.1678-9199http://hdl.handle.net/11449/11651S1678-91992011000100004WOS:000288385200004S1678-91992011000100004-en.pdf9353490382598257Web of Sciencereponame:Repositório Institucional da UNESPinstname:Universidade Estadual Paulista (UNESP)instacron:UNESPengJournal of Venomous Animals and Toxins Including Tropical Diseases1.7820,573info:eu-repo/semantics/openAccess2024-04-11T15:28:17Zoai:repositorio.unesp.br:11449/11651Repositório InstitucionalPUBhttp://repositorio.unesp.br/oai/requestopendoar:29462024-04-11T15:28:17Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP)false |
dc.title.none.fl_str_mv |
Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom |
title |
Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom |
spellingShingle |
Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom Barros, L. C. [UNESP] gyroxin neurotoxicity coagulant activity Crotalus durissus terrificus serine proteinase |
title_short |
Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom |
title_full |
Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom |
title_fullStr |
Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom |
title_full_unstemmed |
Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom |
title_sort |
Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom |
author |
Barros, L. C. [UNESP] |
author_facet |
Barros, L. C. [UNESP] Soares, A. M. Costa, F. L. Rodrigues, V. M. Fuly, A. L. Giglio, J. R. Gallacci, Marcia [UNESP] Thomazini-Santos, I. A. [UNESP] Barraviera, Silvia Regina Catharino Sartori [UNESP] Barraviera, Benedito [UNESP] Ferreira Júnior, Rui Seabra [UNESP] |
author_role |
author |
author2 |
Soares, A. M. Costa, F. L. Rodrigues, V. M. Fuly, A. L. Giglio, J. R. Gallacci, Marcia [UNESP] Thomazini-Santos, I. A. [UNESP] Barraviera, Silvia Regina Catharino Sartori [UNESP] Barraviera, Benedito [UNESP] Ferreira Júnior, Rui Seabra [UNESP] |
author2_role |
author author author author author author author author author author |
dc.contributor.none.fl_str_mv |
Universidade Estadual Paulista (Unesp) Universidade de São Paulo (USP) Universidade Federal de Uberlândia (UFU) Universidade Federal Fluminense (UFF) |
dc.contributor.author.fl_str_mv |
Barros, L. C. [UNESP] Soares, A. M. Costa, F. L. Rodrigues, V. M. Fuly, A. L. Giglio, J. R. Gallacci, Marcia [UNESP] Thomazini-Santos, I. A. [UNESP] Barraviera, Silvia Regina Catharino Sartori [UNESP] Barraviera, Benedito [UNESP] Ferreira Júnior, Rui Seabra [UNESP] |
dc.subject.por.fl_str_mv |
gyroxin neurotoxicity coagulant activity Crotalus durissus terrificus serine proteinase |
topic |
gyroxin neurotoxicity coagulant activity Crotalus durissus terrificus serine proteinase |
description |
Gyroxin, a thrombin-like enzyme isolated from Crotalus durissus terrificus venom and capable of converting fibrinogen into fibrin, presents coagulant and neurotoxic activities. The aim of the present study was to evaluate such coagulant and toxic properties. Gyroxin was isolated using only two chromatographic steps - namely gel filtration (Sephadex G-75) and affinity (Benzamidine Sepharose 6B) -resulting in a sample of high purity, as evaluated by RP-HPLC C2/C18 and electrophoretic analysis that showed a molecular mass of 30 kDa. Gyroxin hydrolyzed specific chromogenic substrates, which caused it to be classified as a serine proteinase and thrombin-like enzyme. It was stable from pH 5.5 to 8.5 and inhibited by Mn(2)+, Cu(2)+, PMSF and benzamidine. Human plasma coagulation was more efficient at pH 6.0. An in vivo toxicity test showed that only behavioral alterations occurred, with no barrel rotation. Gyroxin was not able to block neuromuscular contraction in vitro, which suggests that its action, at the studied concentrations, has no effect on the peripheral nervous system. |
publishDate |
2011 |
dc.date.none.fl_str_mv |
2011-01-01 2014-05-20T13:34:02Z 2014-05-20T13:34:02Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://dx.doi.org/10.1590/S1678-91992011000100004 Journal of Venomous Animals and Toxins Including Tropical Diseases. Botucatu: Cevap-unesp, v. 17, n. 1, p. 23-33, 2011. 1678-9199 http://hdl.handle.net/11449/11651 S1678-91992011000100004 WOS:000288385200004 S1678-91992011000100004-en.pdf 9353490382598257 |
url |
http://dx.doi.org/10.1590/S1678-91992011000100004 http://hdl.handle.net/11449/11651 |
identifier_str_mv |
Journal of Venomous Animals and Toxins Including Tropical Diseases. Botucatu: Cevap-unesp, v. 17, n. 1, p. 23-33, 2011. 1678-9199 S1678-91992011000100004 WOS:000288385200004 S1678-91992011000100004-en.pdf 9353490382598257 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
Journal of Venomous Animals and Toxins Including Tropical Diseases 1.782 0,573 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
23-33 application/pdf |
dc.publisher.none.fl_str_mv |
Universidade Estadual Paulista (Unesp), Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP) |
publisher.none.fl_str_mv |
Universidade Estadual Paulista (Unesp), Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP) |
dc.source.none.fl_str_mv |
Web of Science reponame:Repositório Institucional da UNESP instname:Universidade Estadual Paulista (UNESP) instacron:UNESP |
instname_str |
Universidade Estadual Paulista (UNESP) |
instacron_str |
UNESP |
institution |
UNESP |
reponame_str |
Repositório Institucional da UNESP |
collection |
Repositório Institucional da UNESP |
repository.name.fl_str_mv |
Repositório Institucional da UNESP - Universidade Estadual Paulista (UNESP) |
repository.mail.fl_str_mv |
|
_version_ |
1797789544802680832 |