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

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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Main Authors: Barros,LC, Soares,AM, Costa,FL, Rodrigues,VM, Fuly,AL, Giglio,JR, Gallacci,M, Thomazini-Santos,IA, Barraviera,SRCS, Barraviera,B, Ferreira Junior,RS
Format: Digital revista
Language:English
Published: Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP) 2011
Online Access:http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100004
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spelling oai:scielo:S1678-919920110001000042011-03-01Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venomBarros,LCSoares,AMCosta,FLRodrigues,VMFuly,ALGiglio,JRGallacci,MThomazini-Santos,IABarraviera,SRCSBarraviera,BFerreira Junior,RS gyroxin neurotoxicity coagulant activity Crotalus durissus terrificus serine proteinase 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.info:eu-repo/semantics/openAccessCentro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)Journal of Venomous Animals and Toxins including Tropical Diseases v.17 n.1 20112011-01-01info:eu-repo/semantics/articletext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100004en10.1590/S1678-91992011000100004
institution SCIELO
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country Brasil
countrycode BR
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access En linea
databasecode rev-scielo-br
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region America del Sur
libraryname SciELO
language English
format Digital
author Barros,LC
Soares,AM
Costa,FL
Rodrigues,VM
Fuly,AL
Giglio,JR
Gallacci,M
Thomazini-Santos,IA
Barraviera,SRCS
Barraviera,B
Ferreira Junior,RS
spellingShingle Barros,LC
Soares,AM
Costa,FL
Rodrigues,VM
Fuly,AL
Giglio,JR
Gallacci,M
Thomazini-Santos,IA
Barraviera,SRCS
Barraviera,B
Ferreira Junior,RS
Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom
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_sort Barros,LC
title Biochemical and biological evaluation of gyroxin isolated from Crotalus durissus terrificus venom
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
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.
publisher Centro de Estudos de Venenos e Animais Peçonhentos (CEVAP/UNESP)
publishDate 2011
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1678-91992011000100004
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