Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom

Detalhes bibliográficos
Autor(a) principal: Barros,LC
Data de Publicação: 2011
Outros Autores: Soares,AM, Costa,FL, Rodrigues,VM, Fuly,AL, Giglio,JR, Gallacci,M, Thomazini-Santos,IA, Barraviera,SRCS, Barraviera,B, Ferreira Junior,RS
Tipo de documento: Artigo
Idioma: eng
Título da fonte: The Journal of venomous animals and toxins including tropical diseases (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100004
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 Mn²+, Cu²+, 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.
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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 Mn²+, Cu²+, 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.Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)2011-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100004Journal of Venomous Animals and Toxins including Tropical Diseases v.17 n.1 2011reponame:The Journal of venomous animals and toxins including tropical diseases (Online)instname:Universidade Estadual Paulista (UNESP)instacron:UNESP10.1590/S1678-91992011000100004info:eu-repo/semantics/openAccessBarros,LCSoares,AMCosta,FLRodrigues,VMFuly,ALGiglio,JRGallacci,MThomazini-Santos,IABarraviera,SRCSBarraviera,BFerreira Junior,RSeng2011-03-01T00:00:00Zoai:scielo:S1678-91992011000100004Revistahttp://www.scielo.br/jvatitdPUBhttps://old.scielo.br/oai/scielo-oai.php||editorial@jvat.org.br1678-91991678-9180opendoar:2011-03-01T00:00The Journal of venomous animals and toxins including tropical diseases (Online) - 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,LC
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,LC
author_facet Barros,LC
Soares,AM
Costa,FL
Rodrigues,VM
Fuly,AL
Giglio,JR
Gallacci,M
Thomazini-Santos,IA
Barraviera,SRCS
Barraviera,B
Ferreira Junior,RS
author_role author
author2 Soares,AM
Costa,FL
Rodrigues,VM
Fuly,AL
Giglio,JR
Gallacci,M
Thomazini-Santos,IA
Barraviera,SRCS
Barraviera,B
Ferreira Junior,RS
author2_role author
author
author
author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Barros,LC
Soares,AM
Costa,FL
Rodrigues,VM
Fuly,AL
Giglio,JR
Gallacci,M
Thomazini-Santos,IA
Barraviera,SRCS
Barraviera,B
Ferreira Junior,RS
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 Mn²+, Cu²+, 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
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100004
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100004
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1678-91992011000100004
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)
publisher.none.fl_str_mv Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)
dc.source.none.fl_str_mv Journal of Venomous Animals and Toxins including Tropical Diseases v.17 n.1 2011
reponame:The Journal of venomous animals and toxins including tropical diseases (Online)
instname:Universidade Estadual Paulista (UNESP)
instacron:UNESP
instname_str Universidade Estadual Paulista (UNESP)
instacron_str UNESP
institution UNESP
reponame_str The Journal of venomous animals and toxins including tropical diseases (Online)
collection The Journal of venomous animals and toxins including tropical diseases (Online)
repository.name.fl_str_mv The Journal of venomous animals and toxins including tropical diseases (Online) - Universidade Estadual Paulista (UNESP)
repository.mail.fl_str_mv ||editorial@jvat.org.br
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