15 research outputs found

    Adaptabilidade e estabilidade de variedades e híbridos de milho no Estado da Bahia no ano agrícola de 1999/2000.

    No full text
    No ano agrícola de 1999/2000 foram avaliados, em uma rede experimental, quarenta e um híbridos de milho e, ao mesmo tempo, em uma outra rede, catorze híbridos e vinte e duas variedades, visando conhecer a adaptabilidade e a estabilidade de comportamento desses materiais para fins de recomendação. Os ensaios foram distribuídos nas principais regiões produtoras de milho do Estado da Bahia, em blocos ao acaso, com três repetições. Em ambas as redes experimentais foram observadas, nas análises de variância conjuntas, diferenças entre as cultivares e comportamento inconsistente dessas cultivares nas diferentes condições ambientais, Os híbridos mostraram melhor comportamento produtivo do que as variedades, expressando melhor adaptabilidade e estabilidade de comportamento. O método utilizado (Lin e Binns modificado por Carneiro, 1998) mostrou-se eficiente na identificação das melhores cultivares, tanto nos ambientes favoráveis quanto nos ambientes desfavoráveis. Os híbridos Zeneca 850 I, Cargill 444, Pioneer 3041 e Dina 1000, dentre outros, mostraram melhor performance nos diferentes tipos de ambientes,200

    Cdna Cloning And 1.75 Å Crystal Structure Determination Of Ppl2, An Endochitinase And N-acetylglucosamine-binding Hemagglutinin From Parkia Platycephala Seeds

    No full text
    Parkia platycephala lectin 2 was purified from Parkia platycephala (Leguminosae, Mimosoideae) seeds by affinity chromatography and RP-HPLC. Equilibrium sedimentation and MS showed that Parkia platycephala lectin 2 is a nonglycosylated monomeric protein of molecular mass 29 407 ± 15 Da, which contains six cysteine residues engaged in the formation of three intramolecular disulfide bonds. Parkia platycephala lectin 2 agglutinated rabbit erythrocytes, and this activity was specifically inhibited by N-acetylglucosamine. In addition, Parkia platycephala lectin 2 hydrolyzed β(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-β-d-glucopyranose units in chitin. The full-length amino acid sequence of Parkia platycephala lectin 2, determined by N-terminal sequencing and cDNA cloning, and its three-dimensional structure, established by X-ray crystallography at 1.75 Å resolution, showed that Parkia platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (βα)8 barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182. © 2006 The Authors.2731739623974Van Damme, E.J.M., Peumans, W.J., Barre, A., Rougé, P., Plant lectins: A composite of several distinct families of structurally and evolutionary related proteins with diverse biological roles (1998) Crit Rev Plant Sci, 17, pp. 575-692Gabius, H.-J., Gabius, S., (1997) Glycoscience. Status and Perspectives, , Chapman & Hall, WeinheimDodd, R.B., Drickamer, K., Lectin-like proteins in model organisms: Implications for evolution of carbohydrate-binding activity (2001) Glycobiology, 11, pp. 71-79Rini, J.M., Lectin structure (1995) Annu Rev Biomol Struct, 24, pp. 551-577Weis, W.I., Drickamer, K., Structural basis of lectin-carbohydrate recognition (1996) Annu Rev Biochem, 65, pp. 441-473Elgavish, S., Shaanan, B., Lectin-carbohydrate interactions: Different folds, common recognition principles (1997) Trends Biochem Sci, 22, pp. 462-467Loris, R., Hamelryck, T., Bouckaert, J., Wyns, L., Legume lectin structure (1998) Biochim Biophys Acta, 1383, pp. 9-36Bouckaert, J., Hamelryck, T., Wyns, L., Loris, R., Novel structures of plant lectins and their complexes with carbohydrates (1999) Curr Opin Struct Biol, 9, pp. 572-577Vijayan, M., Chandra, N., Lectins (1999) Curr Opin Struct Biol, 9, pp. 707-714Chervenak, M.C., Toone, E.J., Calorimetric analysis of the binding of lectins with overlapping carbohydrate binding (1995) Biochemistry, 34, pp. 5685-5695Dam, T.K., Cavada, B.S., Grangeiro, T.B., Santos, C.F., De Sousa, F.A.M., Oscarson, S., Brewer, C.F., Diocleinae lectins are a group of proteins with conserved binding sites for the core trimannoside of asparagine-linked oligosaccharides and differential specificities for complex carbohydrates (1998) J Biol Chem, 273, pp. 12082-12088Dam, T.K., Cavada, B.S., Grangeiro, T.B., Santos, C.F., Ceccatto, V.M., De Sousa, F.A.M., Oscarson, S., Brewer, C.F., Thermodynamic binding studies of lectins from the diocleinae subtribe to deoxy analogs of the core trimannoside of asparagine-linked oligosaccharides (2000) J Biol Chem, 275, pp. 16119-16126Dam, T.K., Roy, R., Das, S.K., Oscarson, S., Brewer, C.F., Binding of multivalent carbohydrates to concanavalin a and Dioclea grandiflora lectin. Thermodynamic analysis of the 'multivalency effect' (2000) J Biol Chem, 275, pp. 14223-14230Suvachittanont, W., Peutpaiboon, A., Lectin from Parkia speciosa seeds (1992) Phytochemistry, 31, pp. 4065-4070Utarabhand, P., Akkayanont, P., Purification of a lectin from Parkia javanica beans (1995) Phytochemistry, 38, pp. 281-285Cavada, B.S., Madeira, S.V.F., Calvete, J.J., Sousa, L.A.G., Bomfim, L.R., Dantas, A.R., Lopes, M.C., Pinto, V.P.T., Purification, chemical, and immunochemical properties of a new lectin from Mimosoideae (Parkia discolor) (2000) Prep Biochem Biotech, 30, pp. 271-280Cavada, B.S., Santos, C.F., Grangeiro, T.B., Moreira Da Silva, L.I.M., Campos, M.J.O., De Sousa, F.A.M., Calvete, J.J., Isolation and partial characterization of a lectin from Parkia platycephala Benth seeds (1997) Physiol Mol Biol Plant, 3, pp. 109-115Ramos, M.V., Cavada, B.S., Bomfim, L.R., Debray, H., Mazard, A.-M., Calvete, J.J., Grangeiro, T.B., Rougé, P., Interaction of the seed lectin from Parkia platycephala (Mimosoideae) with carbohydrates and complex glycans (1999) Prot Pept Lett, 6, pp. 215-222Mann, K., Farias, C.M., Gallego Del Sol, F.G., Santos, C.F., Grangeiro, T.B., Nagano, C.S., Cavada, B.S., Calvete, J.J., The amino-acid sequence of the glucose/mannose-specific lectin isolated from Parkia platycephala seeds reveals three tandemly arranged jacalin-related domains (2001) Eur J Biochem, 268, pp. 4414-4422Gallego Del Sol, F., Gómez, J., Hoos, C., Nagano, C.S., Cavada, B.S., England, P., Calvete, J.J., Energetics of 5-bromo-4-chloro-3-indolyl-α-D-mannose binding to the Parkia platycephala seed lectin and its use for MAD phasing (2005) Acta Cryst F, 61, pp. 326-331Gallego Del Sol, F., Nagano, C.S., Cavada, B.S., Calvete, J.J., The first crystal structure of a Mimosoideae lectin reveals a novel quaternary arrangement of a widespread domain (2005) J Mol Biol, 353, pp. 574-583Heywood, V.H., (1971) Chemotaxonomy of the Leguminosae, pp. 1-29. , Harborne JB & Boulter D, eds, Academic Press, LondonChrispeels, M.J., Raikhel, N.V., Lectins, lectin genes, and their role in plant defense (1991) Plant Cell, 3, pp. 1-9Wang, X., Ma, Q., Characterization of a jasmonate-regulated wheat protein related to a β-glucosidase-aggregating factor (2005) Plant Physiol Biochem, 43, pp. 185-192Collinge, D.B., Kragh, K.M., Mikkelsen, J.D., Nielsen, K.K., Rasmussen, U., Vad, K., Plant chitinases (1993) Plant J, 3, pp. 31-40Hamel, F., Boivin, R., Tremblay, C., Bellemare, G., Structural and evolutionary relationships among chitinases of flowering plants (1997) J Mol Evol, 44, pp. 614-624Kasprzewska, A., Plant chitinases - Regulation and function (2003) Cell Mol Biol Lett, 8, pp. 809-824Cavada, B.S., Castellón, R.E.R., Vasconcelos, G.G., Rocha, B.A.M., Bezerra, G.A., Debray, H., Delatorre, P., Pinto, V.P.T., Crystallization and preliminary X-ray diffraction analysis of a new chitin-binding protein from Parkia platycephala seeds (2005) Acta Crystallogr F, 61, pp. 841-843Rawitch, A.B., Pollock, H.G., Yang, S.-X., Thyroglobulin glycosylation: Location and nature of the N-linked oligosaccharide units in bovine thyroglobulin (1993) Arch Biochem Biophys, 300, pp. 271-279Hill Jr., H.D., Reynolds, J.A., Hill, R.L., Purification, composition, molecular weight, and subunit structure of ovine submaxillary mucin (1977) J Biol Chem, 252, pp. 3791-3798Spiro, R.G., Bhoyroo, D., Structure of the O-glycosidically linked carbohydrate units of fetuin (1974) J Biol Chem, 249, pp. 5704-5717Green, E.D., Adelt, G., Baenziger, J.U., Wilson, S., Van Halbeek, H., The asparagine-linked oligosaccharides on bovine fetuin. Structural analysis of N-glycanase-released oligosaccharide by 500-megahertz1H NMR spectroscopy (1988) J Biol Chem, 263, pp. 18253-18268Rohrer, J.S., Cooper, G.A., Townsend, R.R., Identification, quantitation, and characterization of glycopeptides in reversed-phase HPLC separations of glycoprotein proteolytic digests (1993) Anal Biochem, 212, pp. 7-16Henrissat, B., A classification of glycosyl hydrolases based on amino acid sequence similarities (1991) Biochem J, 280, pp. 309-316Jekel, P.A., Hartmann, B.H., Beintema, J.J., The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex (1991) Eur J Biochem, 200, pp. 123-130Van Scheltinga, A.C.T., Kalk, K.H., Beintema, J.J., Dijkstra, B.W., Crystal structures of hevamine, a plant defense protein with chitinase and lysozyme activity, and its complex with an inhibitor (1994) Structure, 2, pp. 1181-1189Chye, M.L., Zhao, K.J., He, Z.M., Ramalingam, S., Fung, K.L., An agglutinating chitinase with two chitin-binding domains confers fungal protection in transgenic potato (2005) Planta, 220, pp. 717-730Tang, C.M., Chye, M.L., Ramalingam, S., Ouyang, S.W., Zhao, K.J., Ubhayasekera, W., Mowbray, S.L., Functional analyses of the chitin-binding domains and the catalytic domain of Brassica juncea chitinase BjCHI1 (2004) Plant Mol Biol, 56, pp. 285-298Robertus, J.D., Monzingo, A.F., The structure and action of chitinases (1999) EXS, 87, pp. 125-135Kaomek, M., Mizuno, K., Fujimura, T., Sriyotha, P., Cairns, J.R., Cloning, expression, and characterization of an antifungal chitinase from Leucaena leucocephala de Wit (2003) Biosci Biotechnol Biochem, 67, pp. 667-676Hennig, M., Jansonius, J.N., Van Scheltinga, A.C.T., Dijkstra, B.W., Schlesier, B.J., Crystal structure of concanavalin B at 1.65 a resolution. An 'inactivated' chitinase from seeds of Canavalia ensiformis (1995) J Mol Biol, 254, pp. 237-246Van Scheltinga, A.C.T., Hennig, M., Dijkstra, B.W., The 1.8 a ° resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18 (1996) J Mol Biol, 262, pp. 243-257Lawton, K.A., Beck, J., Potter, S., Ward, E., Ryals, J., Regulation of cucumber class III chitinase gene expression (1994) Mol Plant-Microbe Interact, 7, pp. 48-57Copley, R.R., Barton, G.J., A structural analysis of phosphate and sulphate binding sites in proteins. Estimation of propensities for binding and conservation of phosphate binding sites (1994) J Mol Biol, 242, pp. 321-329Bokma, E., Rozeboom, H.J., Sibbald, M., Dijkstra, B.W., Beintema, J.J., Expression and characterization of active site mutants of hevamine, a chitinase from the rubber tree Hevea brasiliensis (2002) Eur J Biochem, 269, pp. 893-901Pastuszak, I., Drake, R., Elbein, A.D., Kidney N-acetylgalactosamine (GalNAc)-1-phosphate kinase, a new pathway of GalNAc activation (1996) J Biol Chem, 271, pp. 20776-20782Ainouz, I.L., Sampaio, A.H., Benevides, N.M.B., Freitas, A.L.P., Costa, F.H.F., Carvalho, M.R., Pinheirojoventino, F., Agglutination of enzyme treated erythrocytes by Brazilian marine algal extracts (1992) Bot Mar, 35, pp. 475-479Schägger, H., Von Jagow, G., Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa (1987) Anal Biochem, 166, pp. 368-379Henrikson, R.L., Meredith, S.C., Amino acid analysis by reversed-phase high-performance liquid chromatography: Precolumn derivatization with phenylisothiocyanate (1984) Anal Biochem, 136, pp. 65-71Steenkamp, J., Wiid, I., Lourens, A., Van Helden, P., Improved method for DNA extraction from Vitis vinifera (1994) Am J Enol Vitic, 45, pp. 102-106Frohman, M.A., Martin, G.R., Rapid amplification of cDNA ends using nested primers (1989) Techniques, 1, pp. 165-170(1994) Acta Cryst, D50, pp. 760-763. , Collaborative Computational Project Number

    Reproductive biology of Steindachnerina insculpta (Fernandez-Yépez) (Teleostei, Curimatidae) in Furnas reservoir, Minas Gerais, Brazil Biologia reprodutiva de Steindachnerina insculpta (Fernandez-Yépez) (Teleostei, Curimatidae) no reservatório de Furnas, Minas Gerais, Brasil

    No full text
    The 'saguiru' Steindachnerina insculpta, a small teleost detritivorous fish species in Furnas reservoir, upper rio Paraná basin, Minas Gerais, Brazil, has a prolonged period of reproductive activity that extends from September to March, with fractionated spawning. During gonadal maturation, the females showed a low hepatosomatic index, suggesting that hepatic substances are possibly transferred from liver to ovaries. During the reproductive period, this fish had lower stomach repletion and coelomic fat indexes, indicating that the species eat less and consume more fat reserves. The weight of the ovaries influenced positively the condition factor (K1), since the lowest K2 values (without the gonads weight), were obtained during maturation, confirming the influence of the weight of the ovaries upon the physiological condition of the females.<br>O 'saguiru' Steindachnerina insculpta, peixe teleósteo detritívoro que ocorre no reservatório de Furnas, bacia do alto Paraná, Minas Gerais, apresenta período reprodutivo prolongado que se estende de setembro a março, com desova parcelada. Durante a maturação gonadal, fêmeas apresentaram baixos valores do índice hepatossomático, sugerindo que possivelmente, substâncias hepáticas são transferidas do fígado para os ovários. Durante o período reprodutivo, os peixes desta espécie apresentam índices de repleção estomacal e de gordura celômica baixos, indicando diminuição da atividade alimentar e consumo de reservas. O peso dos ovários influencia positivamente o fator de condição (K1), uma vez que os mais baixos valores de K2 (sem o peso das gônadas) foram obtidos durante a maturação, confirmando a influência do peso dos ovários na condição fisiológica das fêmeas

    Efeitos do sistema de preparo na compactação do solo, disponibilidade hídrica e comportamento do feijoeiro Effects of soil tillage on soil compaction, available soil water, and development of common bean

    No full text
    Neste trabalho foram avaliados os efeitos dos sistemas de preparo com arado de aiveca, com grade aradora e plantio direto, na compactação do solo, na disponibilidade de água, no desenvolvimento radicular e na produtividade do feijoeiro (Phaseolus vulgaris L.). A área experimental consistiu de um Latossolo Vermelho-Escuro, sob irrigação via pivô central, o que possibilitou dois cultivos ao ano. O preparo com arado propiciou menores valores de resistência à penetração, ao longo do perfil do solo. O preparo com grade condicionou uma camada mais compacta entre 10 e 24 cm de profundidade e, em plantio direto, houve maior compactação até 15 - 22 cm. A distribuição do sistema radicular, em profundidade, foi mais uniforme no preparo com arado. No preparo com grade houve concentração das raízes na camada de 0-10 cm de profundidade e, em plantio direto, a concentração ocorreu até 20 cm. Sob irrigação, a menor resistência do solo à penetração e a melhor distribuição do sistema radicular, no preparo com arado, não possibilitou ao feijoeiro obter maior produtividade em relação aos outros sistemas de preparo. A maior produtividade observada no plantio direto deveu-se, entre outros fatores, aos menores valores e à menor variação ao longo do ciclo da tensão matricial da água no solo, em comparação aos demais sistemas de preparo do solo.<br>The effects of three tillage methods (moldboard ploughing, disking, and no-tillage) on soil compaction, available soil water, root development, and common bean (Phaseolus vulgaris L.) yield were evaluated. The experiment was carried out on a Dark Red Latosol, under center pivot sprinkler irrigation, which allows cropping twice a year. The soil under moldboard ploughing showed the lowest resistance to penetration throughout the profile, whereas under disking the soil showed a compacted layer between 10 and 24 cm deep. Higher compaction until 15-22 cm was observed under no-tillage. Crop roots were more uniformly distributed throughout the soil profile under moldboard ploughing, whereas under disking and no-tillage roots concentrated in the top 10 and 20 cm of soil, respectively. The lowest resistance to penetration and the more uniform root distribution throughout the soil profile under moldboard ploughing did not reflect on higher yield of common bean as compared to the other tillage methods, when under irrigation. The highest yield observed under no-tillage was due, in part, to the lower values of soil water matrix tension observed, and to the smaller variation in this parameter all over the crop cycle, as opposed to the other methods of soil tillage

    Nitrogen fertilization and soil management of winter common bean crop Manejo do solo e adubação nitrogenada em feijoeiro de inverno

    Get PDF
    The adoption of appropriate cultural management, which includes nitrogen fertilization and soil tillage system, is very important to increase the efficiency of plant in the utilization of available resource. This research work was conducted for three years aiming at evaluating the effect of sidedressing nitrogen application (0, 25, 50, 75, and 100 kg ha-1) on winter bean crop under different systems of soil management (conventional, minimal, and no-tillage systems). The experimental design was a randomized block arranged in strips relative to tillage systems, with random distribution of nitrogen doses into each strip, with four replications. Grain yield was affected by nitrogen rates and significant increases were obtained with the application of 75 to 100 kg N ha-1. Soil management did not affect grain yield, although the "minimum system" provided better results in the two first years.<br>A adoção de manejo cultural adequado, dentro do qual se insere a prática da adubação e do preparo do solo, é importante no sentido de aumentar a eficiência da planta na utilização dos recursos disponíveis. Este trabalho foi desenvolvido durante três anos, objetivando avaliar, no feijoeiro irrigado (Phaseolus vulgaris) "de inverno", o efeito da aplicação de doses de nitrogênio em cobertura (0, 25, 50, 75 e 100 kg ha-1), sob diferentes sistemas de preparo de solo (convencional, mínimo e direto). O delineamento estatístico utilizado foi em blocos casualisados dispostos em faixas para os sistemas de preparo do solo, com casualização dentro destes para as doses de nitrogênio, com quatro repetições. Foram avaliados: florescimento pleno, matéria seca de plantas, número de vagens e de grãos por planta, número de grãos por vagem, massa de 100 grãos, ciclo, rendimento de grãos e teor de nitrogênio nas plantas. O rendimento de grãos foi influenciado pelas doses de nitrogênio e incrementos significativos foram obtidos com a aplicação de 75 a 100 kg N ha-1. Os sistemas de preparo do solo não influenciaram no rendimento de grãos, embora o "cultivo mínimo" tenha se sobressaído nos dois primeiros anos
    corecore