11 research outputs found

    Ecomorphological correlates of twenty dominant fish species of Amazonian floodplain lakes

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    Fishes inhabiting Amazonian floodplain lakes exhibits a great variety of body shape, which was a key advantage to colonize the several habitats that compose these areas adjacent to the large Amazon rivers. In this paper, we did an ecomorphological analysis of twenty abundant species, sampled in May and August 2011, into two floodplain lakes of the lower stretch of the Solimões River. The analysis detected differences among species, which could be probably associated with swimming ability and habitat use preferences. © 2017, Instituto Internacional de Ecologia. All rights reserved

    Regulatory Effects Of An Inhibitor From Plathymenia Foliolosa Seeds On The Larval Development Of Anagasta Kuehniella (lepidoptera)

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    The Mediterranean flour moth, Anagasta kuehniella, is one of the most important insect pests of grains, reported worldwide, feeding on stored grains and products of rice, rye, corn and wheat. Plants synthesize a variety of molecules, including trypsin inhibitors, to defend themselves against attack by insects. In this study, a trypsin inhibitor (PFTI) was purified from Plathymenia foliolosa (Benth.) seeds and was tested for insect growth regulatory effect. The survival and mass of A. kuehniella larvae feeding on control seeds were about 82.7% and 5 mg, respectively, whereas survival on seeds containing 0.7% PFTI was about 56%, while a 66.1% reduction in the average mass of the larvae was observed. The results from dietary utilization experiments with A. kuehniella larvae showed a reduction in efficiency of conversion of ingested food and digested food, and an increase in approximate digestibility and metabolic cost. The level of trypsin was significantly decreased in larval midgut and increased in the feces of larvae reared on a diet containing 0.7% PFTI. Results indicate that PFTI possesses a toxic effect against A. kuehniella larvae. © 2008 Elsevier Inc. All rights reserved.1522255261Abdeen, A., Virgos, A., Olivella, E., Villanueva, J., Aviles, X., Gabarra, R., Prat, S., Multiple insect resistance in transgenic tomato plant over-expressing two families of plant proteinase inhibitors (2005) Plant Mol. Biol., 57, pp. 189-202Bhattacharyya, A., Mazumdar, S., Leighton, S.M., Babu, C.R., A Kunitz proteinase inhibitor from Archidendron ellipticum seeds: purification, characterization, and kinetic properties (2006) Phytochemistry, 67, pp. 232-241Bolter, C.J., Jongsman, M.A., Colorado potato beetles (Leptinotarsa decemlineata) adapt to proteinase-inhibitors induced in potato leaves by methyl jasmonate (1995) J. Insect Physiol., 41, pp. 1071-1078Botella, M.A., Xu, Y., Prabha, T.N., Zhao, Y., Narasimhan, M.L., Wilson, K.A., Nielsen, S.S., Hasegawa, P.A., Differential expression of soybean cysteine proteinase inhibitor genes during development and in response to wounding and methyl jasmonate (1996) Plant Physiol., 112, pp. 1201-1210Bradford, M.M., A rapid and sensitive method for the quantification of microgram quantities of protein using the principle of protein-dye binding (1976) Anal. Biochem., 72, pp. 248-254Brito, L.O., Lopes, A.R., Parra, J.R.P., Terra, W.R., Silva-Filho, M.C., Adaptation of tobacco budworm Heliothis virescens to proteinase inhibitors may be mediated by synthesis of new proteinases (2001) Comp. Biochem. Physiol. B, 128, pp. 365-375Broadway, R.M., Duffey, S.S., Plant proteinase inhibitors: mechanism of action and effect on the growth and digestive physiology of larval Heliothis zea and Spodoptera exigua (1986) J. 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Am., 82, pp. 593-598Ferry, N., Edwards, M.G., Gatehouse, J.A., Gatehouse, A.M.R., Plant-insect interactions: molecular approaches to insect resistance (2004) Curr Opinion Biotechnol, 15, pp. 155-161Ferry, N., Edwards, M.G., Gatehouse, T., Capell, P., Christou, P., Gatehouse, A.M.R., Transgenic plants for insect pest control: a forward looking scientific perspective (2006) Transgenic Res., 15, pp. 13-19Garcia, V.A., Freire, M.G.M., Novello, J.C., Marangoni, S., Macedo, M.L.R., Trypsin inhibitor from Poecilanthe parviflora seeds: purification, characterization, and activity against pest proteases (2004) Protein J., 23, pp. 343-350Giri, A.P., Harsulkar, A.M., Desphande, V.V., Sainani, M.N., Gupta, V.S., Ranjekar, P.K., Chickpea defensive proteinase inhibitors can be inactivated by podborer gut proteinases (1998) Plant Physiol., 116, pp. 393-401Haq, S.K., Atif, S.M., Khan, R.H., Protein proteinase inhibitor genes in combat against insects, pests, and pathogens: natural and engineered phytoprotection (2004) Arch. 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Biochem., 49, pp. 593-626Macedo, M.L.R., Xavier-Filho, J., Purification and characterization of trypsin inhibitors from seeds of Clitoria ternatea (1992) J. Sci. Food Agric., 58, pp. 55-58Macedo, M.L.R., Matos, D.G.G., Machado, O.L.T., Marangoni, S., Novello, J.C., Trypsin inhibitors from Dimorphandra mollis seeds: purification and properties (2000) Phytochemistry, 54, pp. 553-558Macedo, M.L.R., Freire, M.G.M., Cabrini, E.C., Toyama, M.H., Novello, J.C., Marangoni, S., A trypsin inhibitor from Peltophorum dubium seeds active against pest proteases and its effect on the survival of Anagasta kuehniella (Lepidoptera: Pyralidae) (2003) Biochim Biophys. Acta, 1621, pp. 170-181Macedo, M.L.R., Freire, M.G.M., Silva, M.B.R., Coelho, L.C.B.B., Insecticidal action of Bauhinia monandra leaf lectin (BmoLL) against Anagasta kuehniella (Lepidoptera: Pyralidae), Zabrotes subfasciatus and Callosobruchus maculatus (Coleoptera: Bruchidae) (2006) Comp. Biochem. Physiol., A146, pp. 486-498Mello, G.C., Oliva, M.L.V., Sumikawa, J.T., Machado, O.L.T., Marangoni, S., Novello, J.C., Macedo, M.L.R., Purification and characterization of a new trypsin inhibitor from Dimorphandra mollis seeds (2001) J. Protein Chem., 20, pp. 625-632Michaud, D., Faye, L., Yelle, S., Electrophoretic analysis of plant cysteine and serine proteinases using gelatin-containing polyacrylamide gels and class-specific proteinase inhibitors (1993) Electrophoresis, 14, pp. 94-99Michaud, D., Bernier-Vadnais, N., Overney, S., Yelle, S., Constitutive expression of digestive cysteine proteinase forms during development of the Colorado potato beetle, Leptinotarsa decemlineata Say (Coleoptera: Chrysomelidae) (1995) Insect Biochem. Mol. Biol., 25, pp. 1041-1048Mordue (Luntz), A., Blackwell, A.J., Azadirachtin: an update (1993) J. Insect Physiol., 39, pp. 903-924Mosolov, V.V., Gricogeva, L.I., Valueva, T.A., Involvement of proteolytic enzymes and their inhibitors in plant protection (review) (2001) Appl. Biochem. Microbiol., 37, pp. 115-123Pando, S.C., Oliva, M.L.V., Sampaio, C.A.M., Di Ciero, L., Novello, J.C., Marangoni, S., Primary sequence determination of a Kunitz inhibitor isolated from Delonix regia seeds (2001) Phytochemistry, 57, pp. 625-631Paulillo, L.C.M.S., Lopes, A.R., Cristofoletti, P.T., Parra, J.R.P., Terra, W.R., Silva-Filho, M.C., Changes in midgut-endopeptidases activity of Spodoptera frugiperda (Lepidoptera: Noctuidae) are responsible for adaptation to soybean proteinase inhibitors (2000) J. Econ. Entomol., 93, pp. 892-896Pompermayer, P., Lopes, A.R., Terra, W.R., Parra, J.R.P., Falco, M.C., Silva-Filho, M.C., Effects of soybean proteinase inhibitor on development, survival and reproductive potential of the sugarcane borer, Diatraea saccharalis (2001) Entomol. Exp. 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    USING SITES FROM INTERNET IN THE CHEMISTY TEACHING AND THEIR ADVANTAGES AND DISADVANTAGES

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    The main goal of this work is to evaluate how the use of the Internet by Chemistry teachers from the City of  Campos dos Goytacazes/RJ, is done as a helping tool in the teaching-learning process. For this purpose, contents of General Chemistry made available in web sites were examined and analyzed, throughout qualitative research, the frequency and the form Chemistry teachers from public schools of Campos of Goytacazes (RJ) manage the contents made available in the Internet. The research data shows that 58% of the teachers have a frequency of individual use of the computer being connected to the Internet daily. 43% of the teachers interviewed already affirmed to have used the resource at once in classroom and 78% already declared to have found contradictions in the information they have researched in sites containing Chemistry information. However, only 38% of the teachers affirmed to check the contents found in the Internet with those made available in text books. Regarding the analyzed sites (6 sites) , none of them was considered excellent taking into account reliability parameters proposed by Hung (2004), like truthfulness, objectivity, present time and authority. Therefore teachers and students should be aware of the advantages and disadvantages Internet can bring to the teaching-learning process so together they can establish necessary guidelines in order to good initial propositions regarding this process do not turn out as self-defeating

    Isolation And Characterization Of A Lectin From Annona Muricata Seeds

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    A lectin with a high affinity for glucose/mannose was isolated from Annona muricata seeds (Annonaceae) by gel filtration chromatography on Sephacryl S-200, ion exchange chromatography on a DEAE SP-5 PW column, and molecular exclusion on a Protein Pak Glass 300 SW column. Sodium dodecyl sulfate polyacrylamide gel electrophoresis (PAGE) yielded two protein bands of approximately 14 kDa and 22 kDa. However, only one band was seen in native PAGE. The Mr of the lectin estimated by fast-performance liquid chromatography-gel filtration on Superdex 75 was 22 kDa. The lectin was a glycoprotein with 8% carbohydrate (neutral sugar) and required divalent metal cations (Ca2+, Mg 2+, and Mn2+) for full activity. Amino acid analysis revealed a large content of Glx, Gly, Phe, and Lys. The lectin agglutinated dog, chicken, horse, goose, and human erythrocytes and inhibited the growth of the fungi Fusarium oxysporum, Fusarium solani, and Colletotrichum musae. © 2003 Plenum Publishing Corporation.2207/08/15655661Allen, A.K., Neuberger, A., Sharon, N., (1973) Biochem. J., 131, pp. 155-162Bones, C., Loiseau, P., Cortes, D., Myint, S.H., Hocquemiller, R., Gayral, P., (1991) Plant Med., 57, pp. 434-436Bradford, M.M., (1976) Anal. Biochem., 72, pp. 248-254Branch, L.C., Silva, I.M.F., (1983) Acta Amazônica., 13, pp. 737-797Coelho, M.B., Freire, M.G.M., Toyama, M.H., Marangoni, S., Novello, J.C., Macedo, M.L.R., (2003) Protein and Peptide Letter, 10, pp. 1-9Datta, P.K., Figueroa, M.O.D.C.R., Lajolo, F.M., (1991) Plant Physiol., 97, pp. 856-862Dubois, M., Gilles, K.A., Hamilton, J.L., Rebers, P.A., Smith, F., (1956) Anal. Chem, 28, pp. 350-356Freire, M.G.M., Gomes, V.M., Corsini, R.E., Machado, O.L.T., De Simone, S.G., Novello, J.C., (2002) Plant Physiol. Biochem., 40, pp. 61-68Goldstein, I.J., Hughes, R.C., Monsigny, M., Osawa, T., Sharon, N., (1980) Nature, 285, pp. 66-73Gomes, V.M., Da Cunha, M., Miguens, F.C., Fernandes, K.V.S., Rose, T.L., Xavier-Filho, J., (1998) Plant Sci., 138, pp. 81-89Henrikson, R.L., Meredith, S.C., (1984) Anal. Biochem., 136, pp. 65-71Laemmli, U.K., (1970) Nature, 227, pp. 680-685Lis, H., Sharon, N., (1984) Biology of Carbohydrates, pp. 1-85. , Ginsburg, V., and Robbins, P. W. (eds), Wiley, New YorkLis, H., Sharon, N., (1986) Annu. Rev. Biochem., 55, pp. 35-67Moreira, R.A., Monteiro, A.C.O., Horta, A.C.G., Oliveira, J.T.A., Cavada, B.S., (1997) Phytochemistry, 2, pp. 139-144Moreira, R.A., Castelo-Branco, C.C., Monteiro, A.C.O., Tavares, R.O., Beltramini, L.M., (1998) Phytochemistry, 47, pp. 1183-1188Peumans, W.J., Verhaert, P., Pfüller, U., Van Damme, E.J.M., (1984) FEBS Lett., 177, pp. 261-265Sampietro, A.R., Isla, M.I., Quiroga, E.N., Vattuone, M.A., (2001) Plant Sci., 160, pp. 659-667Sharon, N., Lis, H., (1990) FASEB J., 4, pp. 3198-3208Shibuya, N., Goldstein, I.J., Shafer, J.A., Peumans, W.J., Broekaert, W.F., (1986) Arch. Biochem. Biophys., 249, pp. 215-224Singh, R.S., Tiwary, A.K., Kennedy, J.F., (1999) Crit. Rev. Biotechnol., 19, pp. 145-178Utarabhand, P., Akkayamont, P., (1995) Phytochemistry, 38, pp. 281-285Van Damme, E.J.M., Peumans, W.J., Barre, A., Rougé, P., (1998) Crit. Rev. Plant. Sci., 17, pp. 575-692Van Parijs, J., Broekaert, W.F., Goldstein, I.J., Peumans, W.J., (1991) Planta, 183, pp. 258-264Van Parijs, J., Broekaert, W.F., Peumans, W.J., Geuns, J.M., Van Laere, A.J., (1992) Arch. Microbiol., 158, pp. 19-25Wang, H.X., Ng, T.B., Ooi, V.E.C., (1999) Int. J. Biochem. Cell Biol., 31, pp. 595-599Xu, Q., Lu, Y., Wang, X., Gu, H., Chen, Z., (1998) Plant Physiol. Biochem., 36, pp. 899-90

    Inflammatory responses induced in mice by lectin from Talisia esculenta seeds

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    FAPESP - FUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULOCNPQ – CONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICOA novel lectin from Talisia esculenta seeds (TEL) has recently been purified and characterized. In this study we investigated the proinflammatory activity of TEL in mice using both the air-pouch and peritoneal cavity as well as paw oedema models. TEL (10-40 mug) induced significant neutrophil and mononuclear cell recruitment when injected into either mouse air-pouch or peritoneal cavity. The neutrophil accumulation into the air-pouch was dose- and time-dependent with a maximal response at 16 h. returning to control levels at 72 h whereas maximal mononuclear cell accumulation was observed at 24 h after TEL injection. The same profile of neutrophil accumulation was observed when this lectin was injected into mouse peritonea] cavity, although the maximal mononuclear cell recruitment was observed 48 h after TEL injection. Additionally, TEL (12.5-200 mug/paw) caused a dose-dependent mice paw, as evaluated at 4 h after the lectin injection. D-mannose, better than D-glucose, significantly inhibited TEL-induced neutrophil migration into the peritoneal cavity or air-pouch. D-galactose had no effect on TEL-induced neutrophil migration in either cavity studied. On the other hand, D-mannose slightly inhibited the TEL-induced paw oedema. whereas neither D-glucose nor D-galactose affected this phenomenon. In conclusion, our data show that TEL induces neutrophil and mononuclear cell accumulation by a mechanism related to their specific sugar-binding properties423275280FAPESP - FUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULOCNPQ – CONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICOFAPESP - FUNDAÇÃO DE AMPARO À PESQUISA DO ESTADO DE SÃO PAULOCNPQ – CONSELHO NACIONAL DE DESENVOLVIMENTO CIENTÍFICO E TECNOLÓGICOsem informaçãosem informaçã
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