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: | Brazilian Archives of Biology and Technology |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132001000100009 |
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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Brazilian Archives of Biology and Technology |
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Anticholinesterase effect of eserine (physostigmine) in fish and crustacean speciesEserinephysostigmineacetylcholinesterasefishsilverside fishcrustaceanThe 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.Instituto de Tecnologia do Paraná - Tecpar2001-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132001000100009Brazilian Archives of Biology and Technology v.44 n.1 2001reponame:Brazilian Archives of Biology and Technologyinstname:Instituto de Tecnologia do Paraná (Tecpar)instacron:TECPAR10.1590/S1516-89132001000100009info:eu-repo/semantics/openAccessMonserrat,José M.Bianchini,Adaltoeng2001-10-25T00:00:00Zoai:scielo:S1516-89132001000100009Revistahttps://www.scielo.br/j/babt/https://old.scielo.br/oai/scielo-oai.phpbabt@tecpar.br||babt@tecpar.br1678-43241516-8913opendoar:2001-10-25T00:00Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar)false |
dc.title.none.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 M. 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 M. |
author_facet |
Monserrat,José M. Bianchini,Adalto |
author_role |
author |
author2 |
Bianchini,Adalto |
author2_role |
author |
dc.contributor.author.fl_str_mv |
Monserrat,José M. 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.none.fl_str_mv |
2001-03-01 |
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=S1516-89132001000100009 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132001000100009 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/S1516-89132001000100009 |
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 |
Instituto de Tecnologia do Paraná - Tecpar |
publisher.none.fl_str_mv |
Instituto de Tecnologia do Paraná - Tecpar |
dc.source.none.fl_str_mv |
Brazilian Archives of Biology and Technology v.44 n.1 2001 reponame:Brazilian Archives of Biology and Technology instname:Instituto de Tecnologia do Paraná (Tecpar) instacron:TECPAR |
instname_str |
Instituto de Tecnologia do Paraná (Tecpar) |
instacron_str |
TECPAR |
institution |
TECPAR |
reponame_str |
Brazilian Archives of Biology and Technology |
collection |
Brazilian Archives of Biology and Technology |
repository.name.fl_str_mv |
Brazilian Archives of Biology and Technology - Instituto de Tecnologia do Paraná (Tecpar) |
repository.mail.fl_str_mv |
babt@tecpar.br||babt@tecpar.br |
_version_ |
1750318268639346688 |