Characterization of Acetylcholinesterase purified from the Lesser Grain Borer, Rhyzopertha dominica (Coleoptera: Bostrichidae)
Autor(a) principal: | |
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Data de Publicação: | 1997 |
Outros Autores: | , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | LOCUS Repositório Institucional da UFV |
Texto Completo: | https://doi.org/10.1016/S0742-8413(97)00208-9 http://www.locus.ufv.br/handle/123456789/18741 |
Resumo: | Acetylcholinesterase (AChE, EC 3.1.1.7) purified from the lesser grain borer (Rhyzopertha dominica) was significantly inhibited by higher concentrations of the substrates acetylthiocholine (ATC), acetyl-(β-methyl) thiocholine (AβMTC) and propionylthiocholine (PTC). The efficiency of AChE for hydrolyzing different substrates was ATC > AβMTC > PTC > S-butyrylthiocholine. The enzyme activity was completely inhibited by 10−5 M eserine or BW284C51, but was only partially inhibited by ethopropazine at the same concentration. These results confirmed that the purified enzyme was an typical insect AChE. Non-denaturing and SDS polyacrylamide gel electrophoresis (PAGE) showed only one major molecular form in the purified AChE with a molecular weight of about 107,000 prior to reduction and about 56,000 after reduction, suggesting the homodimer of AChE linked with disulfide bonds. |
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Guedes, R. N. C.Zhu, K. Y.Kambhampati, S.Dover, B. A.2018-04-17T10:56:34Z2018-04-17T10:56:34Z1997-10-3007428413https://doi.org/10.1016/S0742-8413(97)00208-9http://www.locus.ufv.br/handle/123456789/18741Acetylcholinesterase (AChE, EC 3.1.1.7) purified from the lesser grain borer (Rhyzopertha dominica) was significantly inhibited by higher concentrations of the substrates acetylthiocholine (ATC), acetyl-(β-methyl) thiocholine (AβMTC) and propionylthiocholine (PTC). The efficiency of AChE for hydrolyzing different substrates was ATC > AβMTC > PTC > S-butyrylthiocholine. The enzyme activity was completely inhibited by 10−5 M eserine or BW284C51, but was only partially inhibited by ethopropazine at the same concentration. These results confirmed that the purified enzyme was an typical insect AChE. Non-denaturing and SDS polyacrylamide gel electrophoresis (PAGE) showed only one major molecular form in the purified AChE with a molecular weight of about 107,000 prior to reduction and about 56,000 after reduction, suggesting the homodimer of AChE linked with disulfide bonds.engComparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinologyv. 119, Issue 2, p. 205-210, February 1998Elsevier Science Inc.info:eu-repo/semantics/openAccessAcetylcholinesteraseAffinity chromatographyEnzyme kineticsEnzyme purificationLesser grain borerMolecular weightRhyzopertha dominicaSubstrate specificityCharacterization of Acetylcholinesterase purified from the Lesser Grain Borer, Rhyzopertha dominica (Coleoptera: Bostrichidae)info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfreponame:LOCUS Repositório Institucional da UFVinstname:Universidade Federal de Viçosa (UFV)instacron:UFVORIGINALartigo.pdfartigo.pdfTexto completoapplication/pdf240970https://locus.ufv.br//bitstream/123456789/18741/1/artigo.pdf1daa365c5d5ca202b74519b648a5fa22MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://locus.ufv.br//bitstream/123456789/18741/2/license.txt8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAILartigo.pdf.jpgartigo.pdf.jpgIM Thumbnailimage/jpeg4999https://locus.ufv.br//bitstream/123456789/18741/3/artigo.pdf.jpg43073e14d655a0362c84955c8d6e9b2bMD53123456789/187412018-04-17 23:00:36.562oai:locus.ufv.br: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Repositório InstitucionalPUBhttps://www.locus.ufv.br/oai/requestfabiojreis@ufv.bropendoar:21452018-04-18T02:00:36LOCUS Repositório Institucional da UFV - Universidade Federal de Viçosa (UFV)false |
dc.title.en.fl_str_mv |
Characterization of Acetylcholinesterase purified from the Lesser Grain Borer, Rhyzopertha dominica (Coleoptera: Bostrichidae) |
title |
Characterization of Acetylcholinesterase purified from the Lesser Grain Borer, Rhyzopertha dominica (Coleoptera: Bostrichidae) |
spellingShingle |
Characterization of Acetylcholinesterase purified from the Lesser Grain Borer, Rhyzopertha dominica (Coleoptera: Bostrichidae) Guedes, R. N. C. Acetylcholinesterase Affinity chromatography Enzyme kinetics Enzyme purification Lesser grain borer Molecular weight Rhyzopertha dominica Substrate specificity |
title_short |
Characterization of Acetylcholinesterase purified from the Lesser Grain Borer, Rhyzopertha dominica (Coleoptera: Bostrichidae) |
title_full |
Characterization of Acetylcholinesterase purified from the Lesser Grain Borer, Rhyzopertha dominica (Coleoptera: Bostrichidae) |
title_fullStr |
Characterization of Acetylcholinesterase purified from the Lesser Grain Borer, Rhyzopertha dominica (Coleoptera: Bostrichidae) |
title_full_unstemmed |
Characterization of Acetylcholinesterase purified from the Lesser Grain Borer, Rhyzopertha dominica (Coleoptera: Bostrichidae) |
title_sort |
Characterization of Acetylcholinesterase purified from the Lesser Grain Borer, Rhyzopertha dominica (Coleoptera: Bostrichidae) |
author |
Guedes, R. N. C. |
author_facet |
Guedes, R. N. C. Zhu, K. Y. Kambhampati, S. Dover, B. A. |
author_role |
author |
author2 |
Zhu, K. Y. Kambhampati, S. Dover, B. A. |
author2_role |
author author author |
dc.contributor.author.fl_str_mv |
Guedes, R. N. C. Zhu, K. Y. Kambhampati, S. Dover, B. A. |
dc.subject.pt-BR.fl_str_mv |
Acetylcholinesterase Affinity chromatography Enzyme kinetics Enzyme purification Lesser grain borer Molecular weight Rhyzopertha dominica Substrate specificity |
topic |
Acetylcholinesterase Affinity chromatography Enzyme kinetics Enzyme purification Lesser grain borer Molecular weight Rhyzopertha dominica Substrate specificity |
description |
Acetylcholinesterase (AChE, EC 3.1.1.7) purified from the lesser grain borer (Rhyzopertha dominica) was significantly inhibited by higher concentrations of the substrates acetylthiocholine (ATC), acetyl-(β-methyl) thiocholine (AβMTC) and propionylthiocholine (PTC). The efficiency of AChE for hydrolyzing different substrates was ATC > AβMTC > PTC > S-butyrylthiocholine. The enzyme activity was completely inhibited by 10−5 M eserine or BW284C51, but was only partially inhibited by ethopropazine at the same concentration. These results confirmed that the purified enzyme was an typical insect AChE. Non-denaturing and SDS polyacrylamide gel electrophoresis (PAGE) showed only one major molecular form in the purified AChE with a molecular weight of about 107,000 prior to reduction and about 56,000 after reduction, suggesting the homodimer of AChE linked with disulfide bonds. |
publishDate |
1997 |
dc.date.issued.fl_str_mv |
1997-10-30 |
dc.date.accessioned.fl_str_mv |
2018-04-17T10:56:34Z |
dc.date.available.fl_str_mv |
2018-04-17T10:56:34Z |
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.uri.fl_str_mv |
https://doi.org/10.1016/S0742-8413(97)00208-9 http://www.locus.ufv.br/handle/123456789/18741 |
dc.identifier.issn.none.fl_str_mv |
07428413 |
identifier_str_mv |
07428413 |
url |
https://doi.org/10.1016/S0742-8413(97)00208-9 http://www.locus.ufv.br/handle/123456789/18741 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartofseries.pt-BR.fl_str_mv |
v. 119, Issue 2, p. 205-210, February 1998 |
dc.rights.driver.fl_str_mv |
Elsevier Science Inc. info:eu-repo/semantics/openAccess |
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Elsevier Science Inc. |
eu_rights_str_mv |
openAccess |
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application/pdf |
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Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology |
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Comparative Biochemistry and Physiology Part C: Pharmacology, Toxicology and Endocrinology |
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LOCUS Repositório Institucional da UFV |
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