Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom
Autor(a) principal: | |
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Data de Publicação: | 2011 |
Outros Autores: | , , , , , , , , , |
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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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 |
_version_ |
1748958539098882048 |