Anticholinesterase effect of eserine (physostigmine) in fish and crustacean species
Autor(a) principal: | |
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Data de Publicação: | 2001 |
Outros Autores: | |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da FURG (RI FURG) |
Texto Completo: | http://repositorio.furg.br/handle/1/1283 |
Resumo: | The kinetic characteristic (Km) of cholinesterase from the crab Chasmagnathus granulata, the shrimp Farfantepenaeus paulensis and the fish Odontesthes bonaeriensis were compared and correlated with the anticholinesterasic effect of eserine (physostigmine). For the crustaceans, the estimated Km values were about 5-8 times higher than that estimated for the fish (0.04 mM). In the crab and the shrimp, the concentration of eserine which inhibited 50% of cholinesterase activity (IC50) was estimated as 5.33x10-4 and 4.33x10-4 mM, respectively. In both cases, it was significantly higher (P < 0.05) than that estimated for the fish larvae (7.43x10-5 mM). A high Km could reflect a lower affinity of the cholinesterase for its natural substrate, acetylcholine, or for substrate analogues such as carbamates and organophosphorous pesticides. If we consider the IC50 for eserine as an index of enzyme susceptibility to pesticide inhibition, the cholinesterase from the fish larvae may be a better useful tool in assays for pesticide biomonitoring than that from crustacean species. |
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Monserrat, José MaríaBianchini, Adalto2011-11-02T22:44:15Z2011-11-02T22:44:15Z2001MONSERRAT, José Maria; BIANCHINI, Adalto. Anticholinesterase effect of eserine (physostigmine) in fish and crustacean species. Brazilian Archives of Biology and Technology, Brasil, v. 44, p. 63-68, 2001. Disponível em:<http://www.scielo.br/pdf/babt/v44n1/a09v44n1.pdf>. Acesso em: 22 ago. 2011.1516-8913http://repositorio.furg.br/handle/1/1283The kinetic characteristic (Km) of cholinesterase from the crab Chasmagnathus granulata, the shrimp Farfantepenaeus paulensis and the fish Odontesthes bonaeriensis were compared and correlated with the anticholinesterasic effect of eserine (physostigmine). For the crustaceans, the estimated Km values were about 5-8 times higher than that estimated for the fish (0.04 mM). In the crab and the shrimp, the concentration of eserine which inhibited 50% of cholinesterase activity (IC50) was estimated as 5.33x10-4 and 4.33x10-4 mM, respectively. In both cases, it was significantly higher (P < 0.05) than that estimated for the fish larvae (7.43x10-5 mM). A high Km could reflect a lower affinity of the cholinesterase for its natural substrate, acetylcholine, or for substrate analogues such as carbamates and organophosphorous pesticides. If we consider the IC50 for eserine as an index of enzyme susceptibility to pesticide inhibition, the cholinesterase from the fish larvae may be a better useful tool in assays for pesticide biomonitoring than that from crustacean species.engEserinePhysostigmineAcetylcholinesteraseFishSilverside fishCrustaceanAnticholinesterase effect of eserine (physostigmine) in fish and crustacean speciesinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleinfo:eu-repo/semantics/openAccessreponame:Repositório Institucional da FURG (RI FURG)instname:Universidade Federal do Rio Grande (FURG)instacron:FURGORIGINALAnticholinesterase effect of eserine (physostigmine) in fish and crustacean species.pdfAnticholinesterase effect of eserine (physostigmine) in fish and crustacean species.pdfapplication/pdf168769https://repositorio.furg.br/bitstream/1/1283/1/Anticholinesterase%20effect%20of%20eserine%20%28physostigmine%29%20in%20fish%20and%20crustacean%20species.pdf417eb901d983ffd84b52668d2c14a509MD51open accessLICENSElicense.txtlicense.txttext/plain; charset=utf-81724https://repositorio.furg.br/bitstream/1/1283/2/license.txt5b92b9704b4f13242d70e45ddef35a68MD52open access1/12832011-11-02 20:44:15.53open accessoai:repositorio.furg.br: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Repositório InstitucionalPUBhttps://repositorio.furg.br/oai/request || http://200.19.254.174/oai/requestopendoar:2011-11-02T22:44:15Repositório Institucional da FURG (RI FURG) - Universidade Federal do Rio Grande (FURG)false |
dc.title.pt_BR.fl_str_mv |
Anticholinesterase effect of eserine (physostigmine) in fish and crustacean species |
title |
Anticholinesterase effect of eserine (physostigmine) in fish and crustacean species |
spellingShingle |
Anticholinesterase effect of eserine (physostigmine) in fish and crustacean species Monserrat, José María Eserine Physostigmine Acetylcholinesterase Fish Silverside fish Crustacean |
title_short |
Anticholinesterase effect of eserine (physostigmine) in fish and crustacean species |
title_full |
Anticholinesterase effect of eserine (physostigmine) in fish and crustacean species |
title_fullStr |
Anticholinesterase effect of eserine (physostigmine) in fish and crustacean species |
title_full_unstemmed |
Anticholinesterase effect of eserine (physostigmine) in fish and crustacean species |
title_sort |
Anticholinesterase effect of eserine (physostigmine) in fish and crustacean species |
author |
Monserrat, José María |
author_facet |
Monserrat, José María Bianchini, Adalto |
author_role |
author |
author2 |
Bianchini, Adalto |
author2_role |
author |
dc.contributor.author.fl_str_mv |
Monserrat, José María Bianchini, Adalto |
dc.subject.por.fl_str_mv |
Eserine Physostigmine Acetylcholinesterase Fish Silverside fish Crustacean |
topic |
Eserine Physostigmine Acetylcholinesterase Fish Silverside fish Crustacean |
description |
The kinetic characteristic (Km) of cholinesterase from the crab Chasmagnathus granulata, the shrimp Farfantepenaeus paulensis and the fish Odontesthes bonaeriensis were compared and correlated with the anticholinesterasic effect of eserine (physostigmine). For the crustaceans, the estimated Km values were about 5-8 times higher than that estimated for the fish (0.04 mM). In the crab and the shrimp, the concentration of eserine which inhibited 50% of cholinesterase activity (IC50) was estimated as 5.33x10-4 and 4.33x10-4 mM, respectively. In both cases, it was significantly higher (P < 0.05) than that estimated for the fish larvae (7.43x10-5 mM). A high Km could reflect a lower affinity of the cholinesterase for its natural substrate, acetylcholine, or for substrate analogues such as carbamates and organophosphorous pesticides. If we consider the IC50 for eserine as an index of enzyme susceptibility to pesticide inhibition, the cholinesterase from the fish larvae may be a better useful tool in assays for pesticide biomonitoring than that from crustacean species. |
publishDate |
2001 |
dc.date.issued.fl_str_mv |
2001 |
dc.date.accessioned.fl_str_mv |
2011-11-02T22:44:15Z |
dc.date.available.fl_str_mv |
2011-11-02T22:44:15Z |
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 |
MONSERRAT, José Maria; BIANCHINI, Adalto. Anticholinesterase effect of eserine (physostigmine) in fish and crustacean species. Brazilian Archives of Biology and Technology, Brasil, v. 44, p. 63-68, 2001. Disponível em:<http://www.scielo.br/pdf/babt/v44n1/a09v44n1.pdf>. Acesso em: 22 ago. 2011. |
dc.identifier.uri.fl_str_mv |
http://repositorio.furg.br/handle/1/1283 |
dc.identifier.issn.none.fl_str_mv |
1516-8913 |
identifier_str_mv |
MONSERRAT, José Maria; BIANCHINI, Adalto. Anticholinesterase effect of eserine (physostigmine) in fish and crustacean species. Brazilian Archives of Biology and Technology, Brasil, v. 44, p. 63-68, 2001. Disponível em:<http://www.scielo.br/pdf/babt/v44n1/a09v44n1.pdf>. Acesso em: 22 ago. 2011. 1516-8913 |
url |
http://repositorio.furg.br/handle/1/1283 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
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reponame:Repositório Institucional da FURG (RI FURG) instname:Universidade Federal do Rio Grande (FURG) instacron:FURG |
instname_str |
Universidade Federal do Rio Grande (FURG) |
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FURG |
institution |
FURG |
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Repositório Institucional da FURG (RI FURG) |
collection |
Repositório Institucional da FURG (RI FURG) |
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