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Registro Completo |
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Biblioteca(s): |
Embrapa Pecuária Sudeste; Embrapa Rondônia; Embrapa Unidades Centrais. |
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Data corrente: |
03/10/2016 |
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Data da última atualização: |
29/11/2016 |
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Tipo da produção científica: |
Artigo em Periódico Indexado |
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Autoria: |
GIGLIOTI, R.; GUIMARÃES, S.; OLIVEIRA-SEQUEIRA, T. C. G.; DAVID, E. B.; BRITO, L. G.; HUACCA, M. E. F.; CHAGAS, A. C. S.; OLIVEIRA, M. C. S. |
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Afiliação: |
LUCIANA GATTO BRITO, CPAF-Rondonia. |
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Título: |
Proteolytic activity of excretory/secretory products of Cochliomyia hominivorax larvae (Diptera: Calliphoridae). |
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Ano de publicação: |
2016 |
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Fonte/Imprenta: |
Pesquisa Veterinária Brasileira, Brasília, DF v. 36, n. 8, p. 711-718, ago. 2016. |
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Idioma: |
Inglês
Português |
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Conteúdo: |
The protein profiles and proteolytic activity of the excretory secretory products (E/SP) of the first (L1), second (L2) and third (L3) larval stages of Cochliomyia hominivorax were studied in the laboratory. Analysis on the E/SP protein profile was carried out using polyacrylamide gel containing sodium dodecyl sulfate (SDS-PAGE). The E/SP of each larval stage (L1, L2 and L3) treated with protease inhibitors, containing 30?g, 40?g and 50?g of protein, was applied to the 10% polyacrylamide gel. The proteolytic activity of the crude E/SP was analyzed in gels copolymerized with gelatin and by colorimetric assays using azocasein as a substrate, with the characterization of the proteases using synthetic inhibitors. Different protein profiles were observed for the larval instars, with L1 presenting the most complex profile. Nevertheless, various protein bands were observed that were common to all the larval instars. The E/SP of all the instars showed proteolytic activity on gelatin, evidenced by proteolysis zones, predominantly with apparently higher molecular masses in L1, while for L2 and L3 the proteolysis zones could also be observed in regions with lower masses. Tests with protease inhibitors using gelatin as substrate showed that the E/SP of larvae were mainly composed of serine proteases. Additionally, inhibition was observed in L2 E/SP treated previously with EDTA, an inhibitor of metalloproteases. The assays with azocasein revealed a gradual increase of proteolytic activity on this substrate with larval development progress, with the strongest inhibitions being observed after treatments with 3,4-dichloroisocoumarin (DCI) for E/SP of L1, L2 and L3. These results suggest that C. hominivorax larvae produce different proteases, a fact that can be related to the parasite?s vital processes for survival, such as penetration into the host?s tissues and nutrition during the larval stage. MenosThe protein profiles and proteolytic activity of the excretory secretory products (E/SP) of the first (L1), second (L2) and third (L3) larval stages of Cochliomyia hominivorax were studied in the laboratory. Analysis on the E/SP protein profile was carried out using polyacrylamide gel containing sodium dodecyl sulfate (SDS-PAGE). The E/SP of each larval stage (L1, L2 and L3) treated with protease inhibitors, containing 30?g, 40?g and 50?g of protein, was applied to the 10% polyacrylamide gel. The proteolytic activity of the crude E/SP was analyzed in gels copolymerized with gelatin and by colorimetric assays using azocasein as a substrate, with the characterization of the proteases using synthetic inhibitors. Different protein profiles were observed for the larval instars, with L1 presenting the most complex profile. Nevertheless, various protein bands were observed that were common to all the larval instars. The E/SP of all the instars showed proteolytic activity on gelatin, evidenced by proteolysis zones, predominantly with apparently higher molecular masses in L1, while for L2 and L3 the proteolysis zones could also be observed in regions with lower masses. Tests with protease inhibitors using gelatin as substrate showed that the E/SP of larvae were mainly composed of serine proteases. Additionally, inhibition was observed in L2 E/SP treated previously with EDTA, an inhibitor of metalloproteases. The assays with azocasein revealed a gradual increase of proteolytic activit... Mostrar Tudo |
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Palavras-Chave: |
Atividade proteolítica; Mosca-da-bicheira; Proteolytic activity; Screw-worm fly. |
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Thesagro: |
Cochliomyia Hominivorax; Díptera; Miiase; Protease. |
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Thesaurus Nal: |
Calliphoridae; Myiasis; Proteinases. |
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Categoria do assunto: |
--
O Insetos e Entomologia |
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URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/148213/1/Proteolytic-activity.pdf
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Marc: |
LEADER 02926naa a2200337 a 4500
001 2057483
005 2016-11-29
008 2016 bl uuuu u00u1 u #d
100 1 $aGIGLIOTI, R.
245 $aProteolytic activity of excretory/secretory products of Cochliomyia hominivorax larvae (Diptera$bCalliphoridae).$h[electronic resource]
260 $c2016
520 $aThe protein profiles and proteolytic activity of the excretory secretory products (E/SP) of the first (L1), second (L2) and third (L3) larval stages of Cochliomyia hominivorax were studied in the laboratory. Analysis on the E/SP protein profile was carried out using polyacrylamide gel containing sodium dodecyl sulfate (SDS-PAGE). The E/SP of each larval stage (L1, L2 and L3) treated with protease inhibitors, containing 30?g, 40?g and 50?g of protein, was applied to the 10% polyacrylamide gel. The proteolytic activity of the crude E/SP was analyzed in gels copolymerized with gelatin and by colorimetric assays using azocasein as a substrate, with the characterization of the proteases using synthetic inhibitors. Different protein profiles were observed for the larval instars, with L1 presenting the most complex profile. Nevertheless, various protein bands were observed that were common to all the larval instars. The E/SP of all the instars showed proteolytic activity on gelatin, evidenced by proteolysis zones, predominantly with apparently higher molecular masses in L1, while for L2 and L3 the proteolysis zones could also be observed in regions with lower masses. Tests with protease inhibitors using gelatin as substrate showed that the E/SP of larvae were mainly composed of serine proteases. Additionally, inhibition was observed in L2 E/SP treated previously with EDTA, an inhibitor of metalloproteases. The assays with azocasein revealed a gradual increase of proteolytic activity on this substrate with larval development progress, with the strongest inhibitions being observed after treatments with 3,4-dichloroisocoumarin (DCI) for E/SP of L1, L2 and L3. These results suggest that C. hominivorax larvae produce different proteases, a fact that can be related to the parasite?s vital processes for survival, such as penetration into the host?s tissues and nutrition during the larval stage.
650 $aCalliphoridae
650 $aMyiasis
650 $aProteinases
650 $aCochliomyia Hominivorax
650 $aDíptera
650 $aMiiase
650 $aProtease
653 $aAtividade proteolítica
653 $aMosca-da-bicheira
653 $aProteolytic activity
653 $aScrew-worm fly
700 1 $aGUIMARÃES, S.
700 1 $aOLIVEIRA-SEQUEIRA, T. C. G.
700 1 $aDAVID, E. B.
700 1 $aBRITO, L. G.
700 1 $aHUACCA, M. E. F.
700 1 $aCHAGAS, A. C. S.
700 1 $aOLIVEIRA, M. C. S.
773 $tPesquisa Veterinária Brasileira, Brasília, DF$gv. 36, n. 8, p. 711-718, ago. 2016.
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Registro original: |
Embrapa Rondônia (CPAF-RO) |
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| 4. |  | SZEWCZYK, B.; BARSKI, P.; SIHLER, W.; RABALSKI, L.; SKRZECZ, I.; HOYOS CARVAJAL, L.; SOUZA, M. L. de. Detection and identification of baculovirus pesticides by multitemperature single-strand conformational polymorphism. Journal of environmental Science and Health Part B, v.53, p. 539-545, 2008.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: Internacional - A |
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| Registros recuperados : 7 | |
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