Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds
Autor(a) principal: | |
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Data de Publicação: | 2005 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UCB |
Texto Completo: | http://twingo.ucb.br:8080/jspui/handle/10869/597 https://repositorio.ucb.br:9443/jspui/handle/123456789/7766 |
Resumo: | Cotton (Gossypium hirsutum L.) is an important agricultural commodity, which is attacked by several pests such as the cotton boll weevil Anthonomus grandis. Adult A. grandis feed on fruits and leaf petioles, reducing drastically the crop production. The predominance of boll weevil digestive serine proteinases has motivated inhibitor screenings in order to discover new ones with the capability to reduce the digestion process. The present study describes a novel proteinase inhibitor from chickpea seeds (Cicer arietinum L.) and its effects against A. grandis. This inhibitor, named CaTI, was purified by using affinity Red-Sepharose Cl-6B chromatography, followed by reversed-phase HPLC (Vydac C18-TP). SDS-PAGE and MALDI-TOF analyses, showed a unique monomeric protein with a mass of 12,877 Da. Purified CaTI showed significant inhibitory activity against larval cotton boll weevil serine proteinases (78%) and against bovine pancreatic trypsin (73%), when analyzed by fluorimetric assays. Although the molecular mass of CaTI corresponded to a-amylase/trypsin bifunctional inhibitors masses, no inhibitory activity against insect and mammalian a-amylases was observed. In order to observe CaTI in vivo effects, an inhibitor rich fraction was added to an artificial diet at different concentrations. At 1.5% (w/w), CaTI caused severe development delay, several deformities and a mortality rate of approximately 45%. These results suggested that CaTI could be useful in the production of transgenic cotton plants with enhanced resistance toward cotton boll weevil. |
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Gomes, Angelica de Paula GalvãoDias, Simoni CamposBloch Junior, CarlosMelo, Francislete RodriguesFurtado Junior, José de RibamarPontes, Rose Gomes Monnerat Solon deSá, Maria Fatima Grossi deFranco, Octávio Luiz2016-10-10T03:52:36Z2016-10-10T03:52:36Z2005GOMES, Angélica de Paula Galvão et al. Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds. Comparative Biochemistry and Physiology, v. 140, n. 2, p. 313-319, 2005.10964959http://twingo.ucb.br:8080/jspui/handle/10869/597https://repositorio.ucb.br:9443/jspui/handle/123456789/7766Cotton (Gossypium hirsutum L.) is an important agricultural commodity, which is attacked by several pests such as the cotton boll weevil Anthonomus grandis. Adult A. grandis feed on fruits and leaf petioles, reducing drastically the crop production. The predominance of boll weevil digestive serine proteinases has motivated inhibitor screenings in order to discover new ones with the capability to reduce the digestion process. The present study describes a novel proteinase inhibitor from chickpea seeds (Cicer arietinum L.) and its effects against A. grandis. This inhibitor, named CaTI, was purified by using affinity Red-Sepharose Cl-6B chromatography, followed by reversed-phase HPLC (Vydac C18-TP). SDS-PAGE and MALDI-TOF analyses, showed a unique monomeric protein with a mass of 12,877 Da. Purified CaTI showed significant inhibitory activity against larval cotton boll weevil serine proteinases (78%) and against bovine pancreatic trypsin (73%), when analyzed by fluorimetric assays. Although the molecular mass of CaTI corresponded to a-amylase/trypsin bifunctional inhibitors masses, no inhibitory activity against insect and mammalian a-amylases was observed. In order to observe CaTI in vivo effects, an inhibitor rich fraction was added to an artificial diet at different concentrations. At 1.5% (w/w), CaTI caused severe development delay, several deformities and a mortality rate of approximately 45%. These results suggested that CaTI could be useful in the production of transgenic cotton plants with enhanced resistance toward cotton boll weevil.Made available in DSpace on 2016-10-10T03:52:36Z (GMT). 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de Publicaçõeshttps://repositorio.ucb.br:9443/jspui/ |
dc.title.pt_BR.fl_str_mv |
Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds |
title |
Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds |
spellingShingle |
Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds Gomes, Angelica de Paula Galvão Serine proteinase inhibitor Cicer arietinum Anthonomus grandis Plant defense Cotton Mass spectrometry Trypsin Digestive enzymes |
title_short |
Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds |
title_full |
Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds |
title_fullStr |
Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds |
title_full_unstemmed |
Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds |
title_sort |
Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds |
author |
Gomes, Angelica de Paula Galvão |
author_facet |
Gomes, Angelica de Paula Galvão Dias, Simoni Campos Bloch Junior, Carlos Melo, Francislete Rodrigues Furtado Junior, José de Ribamar Pontes, Rose Gomes Monnerat Solon de Sá, Maria Fatima Grossi de Franco, Octávio Luiz |
author_role |
author |
author2 |
Dias, Simoni Campos Bloch Junior, Carlos Melo, Francislete Rodrigues Furtado Junior, José de Ribamar Pontes, Rose Gomes Monnerat Solon de Sá, Maria Fatima Grossi de Franco, Octávio Luiz |
author2_role |
author author author author author author author |
dc.contributor.author.fl_str_mv |
Gomes, Angelica de Paula Galvão Dias, Simoni Campos Bloch Junior, Carlos Melo, Francislete Rodrigues Furtado Junior, José de Ribamar Pontes, Rose Gomes Monnerat Solon de Sá, Maria Fatima Grossi de Franco, Octávio Luiz |
dc.subject.por.fl_str_mv |
Serine proteinase inhibitor Cicer arietinum Anthonomus grandis Plant defense Cotton Mass spectrometry Trypsin Digestive enzymes |
topic |
Serine proteinase inhibitor Cicer arietinum Anthonomus grandis Plant defense Cotton Mass spectrometry Trypsin Digestive enzymes |
dc.description.abstract.por.fl_txt_mv |
Cotton (Gossypium hirsutum L.) is an important agricultural commodity, which is attacked by several pests such as the cotton boll weevil Anthonomus grandis. Adult A. grandis feed on fruits and leaf petioles, reducing drastically the crop production. The predominance of boll weevil digestive serine proteinases has motivated inhibitor screenings in order to discover new ones with the capability to reduce the digestion process. The present study describes a novel proteinase inhibitor from chickpea seeds (Cicer arietinum L.) and its effects against A. grandis. This inhibitor, named CaTI, was purified by using affinity Red-Sepharose Cl-6B chromatography, followed by reversed-phase HPLC (Vydac C18-TP). SDS-PAGE and MALDI-TOF analyses, showed a unique monomeric protein with a mass of 12,877 Da. Purified CaTI showed significant inhibitory activity against larval cotton boll weevil serine proteinases (78%) and against bovine pancreatic trypsin (73%), when analyzed by fluorimetric assays. Although the molecular mass of CaTI corresponded to a-amylase/trypsin bifunctional inhibitors masses, no inhibitory activity against insect and mammalian a-amylases was observed. In order to observe CaTI in vivo effects, an inhibitor rich fraction was added to an artificial diet at different concentrations. At 1.5% (w/w), CaTI caused severe development delay, several deformities and a mortality rate of approximately 45%. These results suggested that CaTI could be useful in the production of transgenic cotton plants with enhanced resistance toward cotton boll weevil. |
dc.description.version.pt_BR.fl_txt_mv |
Sim |
dc.description.status.pt_BR.fl_txt_mv |
Publicado |
description |
Cotton (Gossypium hirsutum L.) is an important agricultural commodity, which is attacked by several pests such as the cotton boll weevil Anthonomus grandis. Adult A. grandis feed on fruits and leaf petioles, reducing drastically the crop production. The predominance of boll weevil digestive serine proteinases has motivated inhibitor screenings in order to discover new ones with the capability to reduce the digestion process. The present study describes a novel proteinase inhibitor from chickpea seeds (Cicer arietinum L.) and its effects against A. grandis. This inhibitor, named CaTI, was purified by using affinity Red-Sepharose Cl-6B chromatography, followed by reversed-phase HPLC (Vydac C18-TP). SDS-PAGE and MALDI-TOF analyses, showed a unique monomeric protein with a mass of 12,877 Da. Purified CaTI showed significant inhibitory activity against larval cotton boll weevil serine proteinases (78%) and against bovine pancreatic trypsin (73%), when analyzed by fluorimetric assays. Although the molecular mass of CaTI corresponded to a-amylase/trypsin bifunctional inhibitors masses, no inhibitory activity against insect and mammalian a-amylases was observed. In order to observe CaTI in vivo effects, an inhibitor rich fraction was added to an artificial diet at different concentrations. At 1.5% (w/w), CaTI caused severe development delay, several deformities and a mortality rate of approximately 45%. These results suggested that CaTI could be useful in the production of transgenic cotton plants with enhanced resistance toward cotton boll weevil. |
publishDate |
2005 |
dc.date.issued.fl_str_mv |
2005 |
dc.date.accessioned.fl_str_mv |
2016-10-10T03:52:36Z |
dc.date.available.fl_str_mv |
2016-10-10T03:52:36Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
status_str |
publishedVersion |
format |
article |
dc.identifier.citation.fl_str_mv |
GOMES, Angélica de Paula Galvão et al. Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds. Comparative Biochemistry and Physiology, v. 140, n. 2, p. 313-319, 2005. |
dc.identifier.uri.fl_str_mv |
http://twingo.ucb.br:8080/jspui/handle/10869/597 https://repositorio.ucb.br:9443/jspui/handle/123456789/7766 |
dc.identifier.issn.none.fl_str_mv |
10964959 |
identifier_str_mv |
GOMES, Angélica de Paula Galvão et al. Toxicity to cotton boll weevil Anthonomus grandis of a trypsin inhibitor from chickpea seeds. Comparative Biochemistry and Physiology, v. 140, n. 2, p. 313-319, 2005. 10964959 |
url |
http://twingo.ucb.br:8080/jspui/handle/10869/597 https://repositorio.ucb.br:9443/jspui/handle/123456789/7766 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
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http://www.limpp.com.br/PDFsLIMPP/2005gomes.pdf |
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Restrito UCB info:eu-repo/semantics/openAccess |
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openAccess |
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