Kinetic characterization of gyroxin, a serine protease from Crotalus durissus terrificus venom
Main Author: | |
---|---|
Publication Date: | 2012 |
Other Authors: | , , , , , , , , , |
Format: | Article |
Language: | eng |
Source: | Repositório Institucional da UNIFESP |
Download full: | http://repositorio.unifesp.br/handle/11600/35517 http://dx.doi.org/10.1016/j.biochi.2012.07.020 |
Summary: | This work describes for the first time the characterization of the enzymatic features of gyroxin, a serine protease from Crotalus durissus terrificus venom, capable to induce barrel rotation syndrome in rodents. Measuring the hydrolysis of the substrate ZFR-MCA, the optimal pH for proteolytic cleavage of gyroxin was found to be at pH 8.4. Increases in the hydrolytic activity were observed at temperatures from 25 degrees C to 45 degrees C, and increases of NaCl concentration up to 1 M led to activity decreases. the preference of gyroxin for Arg residues at the substrate P1 position was also demonstrated. Taken together, this work describes the characterization of substrate specificity of gyroxin, as well as the effects of salt and pH on its enzymatic activity. (C) 2012 Elsevier Masson SAS. All rights reserved. |
id |
UFSP_31cdb0a93fa66e213264ac0808471e56 |
---|---|
oai_identifier_str |
oai:repositorio.unifesp.br:11600/35517 |
network_acronym_str |
UFSP |
network_name_str |
Repositório Institucional da UNIFESP |
repository_id_str |
3465 |
spelling |
Yonamine, Camila Miyagui [UNIFESP]Kondo, Marcia Yuri [UNIFESP]Juliano, Maria Aparecida [UNIFESP]Icimoto, Marcelo Yudi [UNIFESP]Baptista, Gandhi R.Yamane, TetsuoOliveira, Vitor [UNIFESP]Juliano, Luiz [UNIFESP]Lapa, Antonio José [UNIFESP]Lima-Landman, Maria Teresa Riggio de [UNIFESP]Hayashi, Mirian Akemi Furuie [UNIFESP]Universidade Federal de São Paulo (UNIFESP)Inst Ciencias Mar UFCUniv Estado Amazonas2016-01-24T14:28:02Z2016-01-24T14:28:02Z2012-12-01Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 94, n. 12, p. 2791-2793, 2012.0300-9084http://repositorio.unifesp.br/handle/11600/35517http://dx.doi.org/10.1016/j.biochi.2012.07.020WOS000312517800039.pdf10.1016/j.biochi.2012.07.020WOS:000312517800039This work describes for the first time the characterization of the enzymatic features of gyroxin, a serine protease from Crotalus durissus terrificus venom, capable to induce barrel rotation syndrome in rodents. Measuring the hydrolysis of the substrate ZFR-MCA, the optimal pH for proteolytic cleavage of gyroxin was found to be at pH 8.4. Increases in the hydrolytic activity were observed at temperatures from 25 degrees C to 45 degrees C, and increases of NaCl concentration up to 1 M led to activity decreases. the preference of gyroxin for Arg residues at the substrate P1 position was also demonstrated. Taken together, this work describes the characterization of substrate specificity of gyroxin, as well as the effects of salt and pH on its enzymatic activity. (C) 2012 Elsevier Masson SAS. All rights reserved.Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Universidade Federal de São Paulo, Dept Farmacol, BR-04044020 São Paulo, BrazilUniversidade Federal de São Paulo, Dept Biofis, BR-04044020 São Paulo, BrazilInst Ciencias Mar UFC, BR-60165081 Fortaleza, Ceara, BrazilUniv Estado Amazonas, Escola Super Ciencias Saude INCT, BR-69065001 Manaus, Amazonas, BrazilUniversidade Federal de São Paulo, Dept Farmacol, BR-04044020 São Paulo, BrazilUniversidade Federal de São Paulo, Dept Biofis, BR-04044020 São Paulo, BrazilWeb of Science2791-2793engElsevier B.V.Biochimiehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policyinfo:eu-repo/semantics/openAccessGyroxinCrotalusKineticEnzymaticSubstrateSpecificityKinetic characterization of gyroxin, a serine protease from Crotalus durissus terrificus venominfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articlereponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPORIGINALWOS000312517800039.pdfapplication/pdf235020${dspace.ui.url}/bitstream/11600/35517/1/WOS000312517800039.pdfaedc817239415435791823e662d714bbMD51open accessTEXTWOS000312517800039.pdf.txtWOS000312517800039.pdf.txtExtracted texttext/plain11707${dspace.ui.url}/bitstream/11600/35517/2/WOS000312517800039.pdf.txt431abb67e2697c9005eedec381570800MD52open access11600/355172023-01-30 22:17:45.973open accessoai:repositorio.unifesp.br:11600/35517Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652023-01-31T01:17:45Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.fl_str_mv |
Kinetic characterization of gyroxin, a serine protease from Crotalus durissus terrificus venom |
title |
Kinetic characterization of gyroxin, a serine protease from Crotalus durissus terrificus venom |
spellingShingle |
Kinetic characterization of gyroxin, a serine protease from Crotalus durissus terrificus venom Yonamine, Camila Miyagui [UNIFESP] Gyroxin Crotalus Kinetic Enzymatic Substrate Specificity |
title_short |
Kinetic characterization of gyroxin, a serine protease from Crotalus durissus terrificus venom |
title_full |
Kinetic characterization of gyroxin, a serine protease from Crotalus durissus terrificus venom |
title_fullStr |
Kinetic characterization of gyroxin, a serine protease from Crotalus durissus terrificus venom |
title_full_unstemmed |
Kinetic characterization of gyroxin, a serine protease from Crotalus durissus terrificus venom |
title_sort |
Kinetic characterization of gyroxin, a serine protease from Crotalus durissus terrificus venom |
author |
Yonamine, Camila Miyagui [UNIFESP] |
author_facet |
Yonamine, Camila Miyagui [UNIFESP] Kondo, Marcia Yuri [UNIFESP] Juliano, Maria Aparecida [UNIFESP] Icimoto, Marcelo Yudi [UNIFESP] Baptista, Gandhi R. Yamane, Tetsuo Oliveira, Vitor [UNIFESP] Juliano, Luiz [UNIFESP] Lapa, Antonio José [UNIFESP] Lima-Landman, Maria Teresa Riggio de [UNIFESP] Hayashi, Mirian Akemi Furuie [UNIFESP] |
author_role |
author |
author2 |
Kondo, Marcia Yuri [UNIFESP] Juliano, Maria Aparecida [UNIFESP] Icimoto, Marcelo Yudi [UNIFESP] Baptista, Gandhi R. Yamane, Tetsuo Oliveira, Vitor [UNIFESP] Juliano, Luiz [UNIFESP] Lapa, Antonio José [UNIFESP] Lima-Landman, Maria Teresa Riggio de [UNIFESP] Hayashi, Mirian Akemi Furuie [UNIFESP] |
author2_role |
author author author author author author author author author author |
dc.contributor.institution.none.fl_str_mv |
Universidade Federal de São Paulo (UNIFESP) Inst Ciencias Mar UFC Univ Estado Amazonas |
dc.contributor.author.fl_str_mv |
Yonamine, Camila Miyagui [UNIFESP] Kondo, Marcia Yuri [UNIFESP] Juliano, Maria Aparecida [UNIFESP] Icimoto, Marcelo Yudi [UNIFESP] Baptista, Gandhi R. Yamane, Tetsuo Oliveira, Vitor [UNIFESP] Juliano, Luiz [UNIFESP] Lapa, Antonio José [UNIFESP] Lima-Landman, Maria Teresa Riggio de [UNIFESP] Hayashi, Mirian Akemi Furuie [UNIFESP] |
dc.subject.eng.fl_str_mv |
Gyroxin Crotalus Kinetic Enzymatic Substrate Specificity |
topic |
Gyroxin Crotalus Kinetic Enzymatic Substrate Specificity |
description |
This work describes for the first time the characterization of the enzymatic features of gyroxin, a serine protease from Crotalus durissus terrificus venom, capable to induce barrel rotation syndrome in rodents. Measuring the hydrolysis of the substrate ZFR-MCA, the optimal pH for proteolytic cleavage of gyroxin was found to be at pH 8.4. Increases in the hydrolytic activity were observed at temperatures from 25 degrees C to 45 degrees C, and increases of NaCl concentration up to 1 M led to activity decreases. the preference of gyroxin for Arg residues at the substrate P1 position was also demonstrated. Taken together, this work describes the characterization of substrate specificity of gyroxin, as well as the effects of salt and pH on its enzymatic activity. (C) 2012 Elsevier Masson SAS. All rights reserved. |
publishDate |
2012 |
dc.date.issued.fl_str_mv |
2012-12-01 |
dc.date.accessioned.fl_str_mv |
2016-01-24T14:28:02Z |
dc.date.available.fl_str_mv |
2016-01-24T14:28:02Z |
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.citation.fl_str_mv |
Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 94, n. 12, p. 2791-2793, 2012. |
dc.identifier.uri.fl_str_mv |
http://repositorio.unifesp.br/handle/11600/35517 http://dx.doi.org/10.1016/j.biochi.2012.07.020 |
dc.identifier.issn.none.fl_str_mv |
0300-9084 |
dc.identifier.file.none.fl_str_mv |
WOS000312517800039.pdf |
dc.identifier.doi.none.fl_str_mv |
10.1016/j.biochi.2012.07.020 |
dc.identifier.wos.none.fl_str_mv |
WOS:000312517800039 |
identifier_str_mv |
Biochimie. Paris: Elsevier France-editions Scientifiques Medicales Elsevier, v. 94, n. 12, p. 2791-2793, 2012. 0300-9084 WOS000312517800039.pdf 10.1016/j.biochi.2012.07.020 WOS:000312517800039 |
url |
http://repositorio.unifesp.br/handle/11600/35517 http://dx.doi.org/10.1016/j.biochi.2012.07.020 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.none.fl_str_mv |
Biochimie |
dc.rights.driver.fl_str_mv |
http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy info:eu-repo/semantics/openAccess |
rights_invalid_str_mv |
http://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
2791-2793 |
dc.publisher.none.fl_str_mv |
Elsevier B.V. |
publisher.none.fl_str_mv |
Elsevier B.V. |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
instname_str |
Universidade Federal de São Paulo (UNIFESP) |
instacron_str |
UNIFESP |
institution |
UNIFESP |
reponame_str |
Repositório Institucional da UNIFESP |
collection |
Repositório Institucional da UNIFESP |
bitstream.url.fl_str_mv |
${dspace.ui.url}/bitstream/11600/35517/1/WOS000312517800039.pdf ${dspace.ui.url}/bitstream/11600/35517/2/WOS000312517800039.pdf.txt |
bitstream.checksum.fl_str_mv |
aedc817239415435791823e662d714bb 431abb67e2697c9005eedec381570800 |
bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 |
repository.name.fl_str_mv |
Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
|
_version_ |
1802764277756461056 |