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Effects of dietary urea levels on milk protein fractions of Holstein cows

AQUINO, A. A.; LIMA, Yv. R.; BOTARO, B. G.; ALBERTO, C. S. S.; PEIXOTO JR., K. C.; SANTOS, M. V.
Fonte: ELSEVIER SCIENCE BV Publicador: ELSEVIER SCIENCE BV
Tipo: Artigo de Revista Científica
Português
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56.04%
The aim of this study was to evaluate the effects of substituting soybean meal for urea on milk protein fractions (casein, whey protein and non-protein nitrogen) of dairy cows in three dietary levels. Nine mid-lactation Holstein cows were used in a 3 x 3 Latin square arrangement, composed of 3 treatments, 3 periods of 21 days each, and 3 squares. The treatments consisted of three different diets fed to lactating cows, which were randomly assigned to three groups of three animals: (A) no urea inclusion, providing 100% of crude protein (CP), rumen undegradable protein (RUP) and rumen degradable protein (RDP) requirements, using soybean meal and sugarcane as roughage; (B) urea inclusion at 7.5 g/kg DM in partial substitution of soybean meal CP equivalent; (C) urea inclusion at 15 g/kg DM in partial substitution of soybean meal CP equivalent. Rations were isoenergetic and isonitrogenous-1 60 g/kg DM of crude protein and 6.40 MJ/kg DM of net energy for lactation. When the data were analyzed by simple polynomial regression, no differences were observed among treatments in relation to milk CP content, true protein, casein, whey protein, non-casein and non-protein nitrogen, or urea. The milk true protein:crude protein and casein:true protein ratios were not influenced by substituting soybean meal for urea in the diet. Based on the results it can be concluded that the addition of urea up to 15 g/kg of diet dry matter in substitution of soybean meal did not alter milk protein concentration casein...

Digestibilidade e propriedades nutricionais do feijão (Phaseolus vulgaris, L.) e de suas proteínas isoladas; Digestibility and nutritional properties of Phaseolus vulgaris, L and itheir major protein fractions

Marquez, Ursula Maria Lanfer
Fonte: Biblioteca Digitais de Teses e Dissertações da USP Publicador: Biblioteca Digitais de Teses e Dissertações da USP
Tipo: Tese de Doutorado Formato: application/pdf
Publicado em 19/05/1988 Português
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66.01%
O estudo da digestibilidade e do aproveitamento biológico do feijão (Phaseolus vulgaris, L. ),variedade Carioca e de suas principais frações protéicas foi realizado em ensaios biológicos com ratos, após tratamento térmico adequado (cocção). À metodologia convencional, baseada no "Ganho de Peso" e na razão entre o N ingerido e excretado, seguiu-se uma técnica utilizando feijões e suas frações protéicas previamente marcadas com 15N e 35S. A ingestão das rações causou respostas diferentes nos animais, específicos para cada fonte protéica. Os animais alimentados com o feijão integral tiveram reduzido aproveitamento biológico e excretaram 34% do nitrogênio ingerido, sendo este valor 3-4 vezes superior ao causado pela ingestão da ração controle de caseína. As frações, albumínicas e glutelínicas, apresentaram valores de "NPR" e "Ganhos de Peso" superiores, apesar de sua relativa baixa digestibilidade (70-80%). A globulina G1, altamente digerível (92%) teve uma utilização biológica muito reduzida, não permitindo o crescimento dos animais. O ensaio biológico do feijão e de suas proteínas, marcados isotopicamente, permitiu diferenciar a origem do nitrogênio e do enxofre fecal, se endógena ou exógena. A concentração de 15N em excesso...

Determinação dos componentes alergênicos da proteina isolada da soja; Determination of allergenic components isolated soy protein

Bittencourt, Alvorita Leite
Fonte: Biblioteca Digitais de Teses e Dissertações da USP Publicador: Biblioteca Digitais de Teses e Dissertações da USP
Tipo: Tese de Doutorado Formato: application/pdf
Publicado em 25/03/2002 Português
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46.15%
O objetivo deste trabalho foi esclarecer qual das frações protéicas da soja é mais alergênica, avaliando-se sua imunogenicidade e alergenicidade por imunoensaios e teste de anafilaxia cutânea passiva. Além desse propósito, este estudo visou a produção de anticorpos monoclonais para utilizá-lo como ferramenta na padronização de um ensaio imunoenzimático com a finalidade de detectar proteínas da soja, em produtos comercializados. A purificação das frações 2S,7S e 11S da soja foi realizada com base em estudos prévios, padronizando-se a metodologia dentro das condições experimentais do laboratório. A constatação da pureza foi realizada por eletroforese em gel de poliacrilamida (gel de empilhamento a 5% e de separação em gradiente de 7 a 15%), onde se verificou as bandas protéicas características de cada fração. Evidenciou-se as subunidades α (63,17 KDa) α' (58,06 KDa) e β (42,09 KDa), correspondentes à fração 7S da soja e as subunidades ácida (38,8 KDa) e básica (21,04 KDa), correspondentes à fração 11S da soja. A fração 2S da soja mostrou uma banda protéica de 20 KDa, nesse ensaio. Os resultados da cinética demonstraram que as frações 7S e 11S da soja são muito imunogênicas...

Nutritional Responses of Rats to Diets Based on Chickpea (Cicer arietinum L.) Seed Meal or Its Protein Fractions

Tavano, Olga Luisa; da Silva, Sinezio Inacio; Demonte, Aureluce; Neves, Valdir Augusto
Fonte: Amer Chemical Soc Publicador: Amer Chemical Soc
Tipo: Artigo de Revista Científica Formato: 11006-11010
Português
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66.04%
The aim of this study was to isolate the protein fractions from chickpea, var. IAC-Marrocos, as well as to evaluate its in vivo nutritional protein quality. Among the proteins, albumins showed better nutritional value in the in vivo assays and amino acid contents, despite their higher trypsin inhibitor contents. Trypsin inhibitors were found to be heat labile in all samples, but the digestibility results for unheated and heated flour and albumins suggest that their contents are not very decisive. The PER values for casein (not supplemented) were very similar to those of heated flour and unheated or heated albumin and total globulins. The albumin and glutelin fractions showed the best results for PDCAAS, however, lower than those of casein. Despite the high digestibility of the globulin the very low essential amino acid content lowered its PDCAAS, and it had the lowest values.

Study of the proteins in the defatted flour and protein concentrate of baru nuts (Dipteryx alata Vog)

Guimarães, Rita de Cássia Avellaneda; Favaro, Simone Palma; Viana, Antonio Camilo Arguelho; Braga Neto, José Antônio; Neves, Valdir Augusto; Honer, Michael Robin
Fonte: Sociedade Brasileira de Ciência e Tecnologia de Alimentos Publicador: Sociedade Brasileira de Ciência e Tecnologia de Alimentos
Tipo: Artigo de Revista Científica Formato: 464-470
Português
Relevância na Pesquisa
56.09%
O baru (Dipteryx alata Vog.) é uma leguminosa abundante no Cerrado brasileiro, cuja castanha pode ser explorada através do uso sustentável para o aproveitamento das frações proteicas e lipídicas. Este trabalho teve como objetivo estudar as proteínas desta castanha, presentes na farinha desengordurada e no concentrado proteico, quanto as suas propriedades funcionais, ao perfil das frações proteicas e à digestibilidade in vitro. A farinha desengordurada com hexano foi submetida à extração no pH de maior solubilidade das proteínas, obtendo-se o concentrado proteico. O perfil eletroforético das frações proteicas foi avaliado em gel de SDS-PAGE. As propriedades funcionais indicaram a possibilidade de emprego em diversos alimentos, assim como a soja, conferindo capacidade de absorção de água, capacidade de absorção de óleo, propriedades emulsificantes e espumabilidade. As globulinas, seguidas das albuminas, são as frações majoritárias da farinha e do concentrado proteico, respectivamente. A digestibilidade foi superior no concentrado em relação à farinha desengordurada.; Baru (Dipteryx alata Vog.) is an abundant legume in the Brazilian Savanna. Its nuts can be exploited sustainably using its protein and lipid fractions. This study aimed to analyze the proteins of the nuts present in the defatted flour and protein concentrate in terms of their functional properties...

Changes in protein fractions, trypsin inhibitor and proteolytic activity in the cotyledons of germinating chickpea

Neves, Valdir Augusto; Lourenço, Euclides Joaquim
Fonte: Universidade Estadual Paulista Publicador: Universidade Estadual Paulista
Tipo: Artigo de Revista Científica Formato: 269-275
Português
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The chickpea seed germination was carried out in 6 days. During the period it was observed a little variation on total nitrogen contents, however the non protein nitrogen was double. A decrease of 19.1 and 20.6% in relation to total nitrogen was observed to the total globulin and albumin fractions, respectively. The gel filtration chromatography on Sepharose CL-6B and SDS-PAGE demonstrated alterations on the distribution patterns of the albumin and total globulin fractions between the initial and the sixth day of germination suggesting the occurrence of protein degradation in the germination process.The assay for acid protease only appeared in the albumin fraction with casein and chickpea total globulin as substrates, whereas the former was more degradated than the latter, however the transformations detected in the protein fractions apppear indicated that others enzymes could be acting during the process. The trypsin inhibitor activity had a little drop after six day of germination indicating a possible increase on the digestibility of the proteins.

Fracionamento da proteína e estudo termoanalítico das leguminosas: grão de bico (Cicer arietinum), variedade Cíciero e tremoço branco (Lupinus albus L.)

Molina, Juliana Prudenciano
Fonte: Universidade Estadual Paulista (UNESP) Publicador: Universidade Estadual Paulista (UNESP)
Tipo: Dissertação de Mestrado Formato: 62 f.
Português
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46.13%
Pós-graduação em Alimentos e Nutrição - FCFAR; No presente trabalho, objetivou-se a determinar a composição química da farinha da semente de grão-de-bico, cultivar Cícero e do tremoço branco; o estabelecimento de condições de extração das proteínas; a separação das diferentes frações protéicas e caracterizou o comportamento térmico das frações protéicas. A composição química da farinha do grão-de-bico revelou valores de 18,72% de proteína, 10,02 % de umidade, 2,96% de cinzas e 2,6% de extrato etéreo. Já a composição química do tremoço revelou valores de 49,88% de proteína, 8,1% de umidade, 1,54% de cinzas e 2,94% de extrato etéreo. As frações do o grão-de-bico, cultivar Cícero, de maior conteúdo protéico foram a globulina com 88,67%, seguida da glutelina 74,78% e albumina 61,69% e prolamina 7,75%. Para o tremoço branco as frações de maiores conteúdos protéicos foram a albumina 91,33%, seguida da glutelina 89,24% e globulina 41,37%. O valor de energia gasta no processo endotérmico para o evento de desnaturação da proteína das frações protéicas do grão-de-bico, cultivar Cícero, expressos em H/Jg-1 é 190,3 para albumina, 154,3 para globulina, 140,4 para glutelina e 35,97 para prolamina. Para as frações protéicas do tremoço branco os valores expressos em H/Jg-1 é 173...

Study of the proteins in the defatted flour and protein concentrate of baru nuts (Dipteryx alata Vog)

Guimarães,Rita de Cássia Avellaneda; Favaro,Simone Palma; Viana,Antonio Camilo Arguelho; Braga Neto,José Antônio; Neves,Valdir Augusto; Honer,Michael Robin
Fonte: Sociedade Brasileira de Ciência e Tecnologia de Alimentos Publicador: Sociedade Brasileira de Ciência e Tecnologia de Alimentos
Tipo: Artigo de Revista Científica Formato: text/html
Publicado em 01/09/2012 Português
Relevância na Pesquisa
56.09%
Baru (Dipteryx alata Vog.) is an abundant legume in the Brazilian Savanna. Its nuts can be exploited sustainably using its protein and lipid fractions. This study aimed to analyze the proteins of the nuts present in the defatted flour and protein concentrate in terms of their functional properties, the profile of their fractions, and the in vitro digestibility. The flour was defatted with hexane and extracted at the pH of higher protein solubility to obtain the protein concentrate. The electrophoretic profile of the protein fractions was evaluated in SDS-PAGE gel. The functional properties of the proteins indicate the possibility of their use in various foods, like soybeans providing water absorption capacity, oil absorption capacity, emulsifying properties, and foamability. Globulins, followed by the albumins, are the major fractions of the flour and protein concentrate, respectively. Digestibility was greater for the concentrate than for the defatted flour.

Immunogenicity and allergenicity of 2S, 7S and 11S soy protein fractions

Bittencourt,Alvorita Leite; Soares,Maria Fernanda de Macedo; Pires,Roberta Ramos; Honmoto,Cristina Sayuri; Tanaka,Márcia Kioko; Jacob,Cristina Miuki Abe; Abdalla,Dulcinéia Saes Parra
Fonte: Divisão de Biblioteca e Documentação do Conjunto das Químicas da Universidade de São Paulo Publicador: Divisão de Biblioteca e Documentação do Conjunto das Químicas da Universidade de São Paulo
Tipo: Artigo de Revista Científica Formato: text/html
Publicado em 01/12/2007 Português
Relevância na Pesquisa
46.15%
It is known that in a part of the population, mainly among children, some are hypersensitive to soybean protein, although it is not yet completely elucidated which protein fraction is more immunogenic/allergenic. The objective of the study was to compare the immunogenicity and allergenicity of the soy protein fractions. The 2S (conglycinin), 7S (beta conglycinin) and 11S (glycinin) fractions were isolated from soy protein by affinity chromatography. These purified soy protein fractions were used as antigens for immunizing BALB/c mice to evaluate their immunogenicity by following the appearance of specific IgM and IgG antibodies in blood serum by ELISA. The allergenicity of these soy protein fractions was evaluated by the following approaches: i) the production of IgE antibodies against 2S, 7S and 11S soy protein fractions by BALBc mice in the anaphylactic cutaneous passive test (PCA), and ii) the production of IgG1 specific antibodies against the 7S fraction in BALB/c mice. The 7S and 11S fractions induced the formation of IgM and IgG antibodies. The PCA test showed that only the 7S fraction was allergenic leading to the production of IgE antibodies. Another evidence that reinforces the allergenicity of the 7S soy protein fraction is the presence of IgG1 specific antibodies reactive to this protein fraction in immunized mice. Our study shows that the 7S soy protein fraction is important to elicit allergic reactions in mice and may contribute to elucidate the allergenicity of soy-derived products.

Chemical composition and crude protein fractions of Coastcross grass under grazing on winter, spring and summer in Southern Brazil

Branco,Antonio Ferriani; Viana,Keila Bianchin; Castañeda,Román David; Prohmann,Paulo Emilio; Coneglian,Sabrina Marcantonio; Mouro,Gisele Fernanda
Fonte: Editora da Universidade Estadual de Maringá - EDUEM Publicador: Editora da Universidade Estadual de Maringá - EDUEM
Tipo: Artigo de Revista Científica Formato: text/html
Publicado em 01/06/2012 Português
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46.11%
The objective of this study work was to assess crude protein fractions in structural components (leaves, stem and dead material) of Coastcross grass (Cynodon dactylon (L.) Pers) under grazing, on winter, spring and summer seasons, in the Northwestern of Paraná, South of Brazil. Were determined CP, NDF, ADF contents and protein fractions, A, B1, B2, B3 and C. The analysis of CP showed great differences among months, but there was no difference among seasons. NDF and ADF in the stem were lower (p < 0.05) during the spring. The season did not affect (p > 0.05) protein fractions A, B1, B2, B3 and C of leaves. However, it was observed that the highest proportions of CP were B3 and A fractions. For the stem, the most important crude protein fraction is A, and it was observed that B1 fraction was lowest (p < 0.05) in the spring. Considering crude protein fractions of the Coastcross grass, in this study conditions, we can conclude that Coastcross grass presents adequate protein value for beef cattle production on pasture.

The effect of chronic ethanol ingestion on synthesis and degradation of soluble, contractile and stromal protein fractions of skeletal muscles from immature and mature rats.

Preedy, V R; Peters, T J
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em 01/04/1989 Português
Relevância na Pesquisa
46.11%
1. An investigation was carried out into the response of soluble, myofibrillar and stromal protein fractions of skeletal muscle to chronic ethanol feeding. Groups of male Wistar rats, of approx. 85 or 280 g body wt., were pair-fed on a nutritionally complete liquid diet containing glucose or a diet in which 36% of the total energy was provided by ethanol. After 6 weeks, rates of protein synthesis were measured with a flooding dose of L-[4-3H]phenylalanine. 2. The protein contents of soluble, myofibrillar and stromal fractions in gastrocnemius muscle from small and large rats were decreased by ethanol feeding. Greater changes were observed in small than in large rats. 3. Fractional synthesis rates of soluble, myofibrillar and stromal proteins of gastrocnemius were all decreased by ethanol treatment. All fractions responded similarly, though percentage decreases in large rats were greater than in small rats. Absolute synthesis rates in gastrocnemius muscles were also decreased after ethanol treatment. All protein fractions responded similarly, and the magnitudes of the responses in large and small rats were also similar. 4. Fractional rates of breakdown, measured by the difference between fractional growth and synthesis rates, were apparently decreased...

Amino acid composition of Lagenaria siceraria seed flour and protein fractions

Ogunbusola, Moriyike Esther; Fagbemi, Tayo Nathaniel; Osundahunsi, Oluwatooyin Faramade
Fonte: Springer-Verlag Publicador: Springer-Verlag
Tipo: Artigo de Revista Científica
Português
Relevância na Pesquisa
46.12%
Defatted seed flours of Lagenaria siceraria (calabash and bottle gourd) were fractionated into their major protein fractions. The amino acid composition of seed flours and their protein fractions were determined and the protein quality was evaluated. Glutamic acid (139–168 mg/g protein) was the most abundant amino acid followed by aspartic acid (89.0–116 mg/g protein) in both the seed flours and their protein fractions. The total essential amino acid ranged from 45.8 to 51.5%. The predicted protein efficiency ratio and the predicted biological value ranged from 2.4 to 2.9 and 8.7 to 44.0, respectively. Lysine and sulphur amino acids were mostly concentrated in the globulin fractions. The first and second limiting amino acids in seed flours and protein fractions were methionine and valine or threonine. The seed flours contained adequate essential amino acids required by growing school children and adults. The seed has potential as protein supplement in cereal based complementary diets or in the replacement of animal proteins in conventional foods.

Genetic variation and environmental effects on beta-conglycinin and glycinin content in Brazilian soybean cultivars

Carrão-Panizzi,Mercedes Concórdia; Kwanyuen,Prachuab; Erhan,Sevim Zeynep; Lopes,Ivani de Oliveira Negrão
Fonte: Embrapa Informação Tecnológica; Pesquisa Agropecuária Brasileira Publicador: Embrapa Informação Tecnológica; Pesquisa Agropecuária Brasileira
Tipo: Artigo de Revista Científica Formato: text/html
Publicado em 01/09/2008 Português
Relevância na Pesquisa
46.14%
The objective of this work was to determine genetic and environmental effects on beta-conglycinin and glycinin content in Brazilian soybean cultivars. The concentrations of these protein fractions were analyzed by scanning densitometry after electrophoresis, in 90 Brazilian soybean cultivars sown in Ponta Grossa, PR, in 2001. The effects of the sowing location were determined in the cultivar MG/BR 46 (Conquista), sown in 16 locations of Goiás and Minas Gerais states (Central Brazil), and in the cultivar IAS 5, sown in 12 locations of Paraná and São Paulo states (Southern Brazil), in 2002 soybean season. A significant variability for beta-conglycinin (7S) and glycinin (11S) protein fractions ratio was observed among the 90 Brazilian soybean cultivars. 'MS/BRS 169' (Bacuri) and 'BR-8' (Pelotas) presented the highest and the lowest 11S/7S ratios (2.76 and 1.17, respectively). Beta-conglycinin protein fractions presented more variability than glycinin protein fractions. Grouping test classified 7S proteins in seven groups, 11S proteins in four groups, and protein fraction ratios (11S/7S) in nine groups. Significant effect of sowing locations was also observed on protein fractions contents. There is a good possibility of breeding for individual protein fractions...

Genetic variation and environmental effects on beta-conglycinin and glycinin content in Brazilian soybean cultivars.

CARRÃO-PANIZZI, M.C.; KWANYUEN, P.; ERHAN, S.Z.; LOPES, I. de O.N.
Fonte: Pesquisa Agropecuária Brasileira, Brasilia, DF, v. 43, n.9, p.1105-1114, set. 2008. Publicador: Pesquisa Agropecuária Brasileira, Brasilia, DF, v. 43, n.9, p.1105-1114, set. 2008.
Tipo: Artigo em periódico indexado (ALICE)
Português
Relevância na Pesquisa
46.14%
The objective of this work was to determine genetic and environmental effects on beta-conglycinin and glycinin content in Brazilian soybean cultivars. The concentrations of these protein fractions were analyzed by scanning densitometry after electrophoresis, in 90 Brazilian soybean cultivars sown in Ponta Grossa, PR, in 2001. The effects of the sowing location were determined in the cultivar MG/BR 46 (Conquista), sown in 16 locations of Goiás and Minas Gerais states (Central Brazil), and in the cultivar IAS 5, sown in 12 locations of Paraná and São Paulo states (Southern Brazil), in 2002 soybean season. A significant variability for beta-conglycinin (7S) and glycinin (11S) protein fractions ratio was observed among the 90 Brazilian soybean cultivars. 'MS/BRS 169' (Bacuri) and 'BR-8' (Pelotas) presented the highest and the lowest 11S/7S ratios (2.76 and 1.17, respectively). Beta-conglycinin protein fractions presented more variability than glycinin protein fractions. Grouping test classified 7S proteins in seven groups, 11S proteins in four groups, and protein fraction ratios (11S/7S) in nine groups. Significant effect of sowing locations was also observed on protein fractions contents. There is a good possibility of breeding for individual protein fractions...

A STUDY OF THE THERAPEUTIC MECHANISM OF ANTIPNEUMOCOCCIC SERUM ON THE EXPERIMENTAL DERMAL PNEUMOCOCCUS INFECTION IN RABBITS : II. A COMPARISON OF THE THERAPEUTIC EFFECT OF UNREFINED, ANTIPNEUMOCOCCIC SERUM WITH THAT OF ITS VARIOUS PROTEIN FRACTIONS: THE RÔLE OF THE NON-ANTIBACTERIAL FACTOR

Sabin, Albert B.
Fonte: The Rockefeller University Press Publicador: The Rockefeller University Press
Tipo: Artigo de Revista Científica
Publicado em 01/01/1933 Português
Relevância na Pesquisa
46.15%
The experiments of the preceding communication showed that the therapeutic action of antipneumococcic serum depends to a considerable extent upon a certain non-antibacterial factor. The experiments reported in the present communication had two main objects; the first was to determine the distribution of the non-antibacterial factor among the various protein fractions of the serum, and incidentally to correlate this property of the factor with that of certain known antibodies, as well as to learn whether or not the protein fractions commonly excluded from refined preparations of antipneumococcic serum, have any therapeutic value; the second was to determine the rôle of the non-antibacterial factor in the therapy of pneumococcus infection, as exemplified by the experimental, dermal, pneumococcus infection in rabbits. To determine the distribution of the non-antibacterial factor, Type I antipneumococcic serum was fractionated with (NH4)2SO4, and the antibacterial bodies were absorbed by concentrated suspensions of heat-killed pneumococci. The activity of the non-antibacterial factor in the different protein fractions was then tested for by adding varying amounts of the absorbed supernatant liquids to a certain constant, subeffective dose of serum. Even though the method of titration has certain inherent faults it was possible to ascertain that the non-antibacterial factor was apparently associated with all the globulin fractions to a similar degree...

Inflammatory mediators and modulators released in organ culture from rabbit skin lesions produced in vivo by sulfur mustard. III. Electrophoretic protein fractions, trypsin-inhibitory capacity, alpha 1-proteinase inhibitor, and alpha 1- and alpha 2-macroglobulin proteinase inhibitors of culture fluids and serum.

Harada, S.; Dannenberg, A. M.; Vogt, R. F.; Myrick, J. E.; Tanaka, F.; Redding, L. C.; Merkhofer, R. M.; Pula, P. J.; Scott, A. L.
Fonte: PubMed Publicador: PubMed
Tipo: Artigo de Revista Científica
Publicado em /01/1987 Português
Relevância na Pesquisa
46.13%
This is the third report in a series on the inflammatory mediators and modulators released in organ culture from skin lesions of various ages, which were produced in vivo in rabbits by the military vesicant, sulfur mustard (SM). It describes the electrophoretic protein fractions and trypsin-inhibitory capacities of the various culture fluids and the amounts of alpha 1-proteinase inhibitor and alpha-macroglobulin proteinase inhibitors in these fluids. With one-dimensional electrophoresis, the albumin and beta-globulin fractions of protein in culture fluids varied little with the development and healing of the SM lesions. These fractions proportionally resembled the corresponding fractions found in serum. The alpha 1-globulin fraction was proportionally smaller than the corresponding fractions of serum as the lesions healed. The alpha 2-globulin fraction was proportionally smaller than the corresponding fractions of serum at all stages of lesion development and healing. The gamma-globulin fraction was proportionally larger as the lesions healed. With two-dimensional electrophoresis, about 68%, 46%, and 35% of the protein spots in culture fluids from representative 1-day and 6-day SM lesions and normal skin, respectively, matched those from serum. In each case...

Fractionation and partial characterization of protein fractions present at different stages of the production of sparkling wines

Luguera, C.; Moreno-Arribas, M. Victoria; Pueyo, E.; Bartolomé, Begoña; Polo, María Carmen
Fonte: Elsevier Publicador: Elsevier
Tipo: Artículo Formato: 24064 bytes; application/msword
Português
Relevância na Pesquisa
66.07%
Soluble proteins from sparkling wines (var. Chardonnay) manufactured industrially following the Champenoise method were analysed by analytical anion-exchange FPLC (fast protein liquid chromatography). Samples of the must, the unfined wine, the fined wine and the sparkling wines after 3, 6, 9, 12, 15 and 18 months of ageing with yeast lees were taken. Eight main must protein fractions were collected and characterized by isoelectric focusing and capillary electrophoresis. Six fractions consisted of proteins with isoelectric points (pIs) from 4.27 to 3.04. Two fractions, according to their UV spectra, seemed to contain phenolic compounds. A comparison of FPLC profiles of the must, the unfined wine and the fined wine indicated that both fermentation and stabilization processes decrease the concentration of those proteins with less affinity for the anion-exchange column and with a higher pi. No changes in the protein profiles of sparkling wines were observed during the first 18 months of ageing with yeast.; Peer reviewed

Immunogenicity and allergenicity of 2S, 7S and 11S soy protein fractions; Imunogenicidade e alergenicidade das frações protéicas 2S, 7S and 11S da soja

Bittencourt, Alvorita Leite; Soares, Maria Fernanda de Macedo; Pires, Roberta Ramos; Honmoto, Cristina Sayuri; Tanaka, Márcia Kioko; Jacob, Cristina Miuki Abe; Abdalla, Dulcinéia Saes Parra
Fonte: Universidade de São Paulo. Faculdade de Ciências Farmacêuticas Publicador: Universidade de São Paulo. Faculdade de Ciências Farmacêuticas
Tipo: info:eu-repo/semantics/article; info:eu-repo/semantics/publishedVersion; Artigo Avaliado pelos Pares Formato: application/pdf
Publicado em 01/12/2007 Português
Relevância na Pesquisa
46.15%
It is known that in a part of the population, mainly among children, some are hypersensitive to soybean protein, although it is not yet completely elucidated which protein fraction is more immunogenic/allergenic. The objective of the study was to compare the immunogenicity and allergenicity of the soy protein fractions. The 2S (conglycinin), 7S (beta conglycinin) and 11S (glycinin) fractions were isolated from soy protein by affinity chromatography. These purified soy protein fractions were used as antigens for immunizing BALB/c mice to evaluate their immunogenicity by following the appearance of specific IgM and IgG antibodies in blood serum by ELISA. The allergenicity of these soy protein fractions was evaluated by the following approaches: i) the production of IgE antibodies against 2S, 7S and 11S soy protein fractions by BALBc mice in the anaphylactic cutaneous passive test (PCA), and ii) the production of IgG1 specific antibodies against the 7S fraction in BALB/c mice. The 7S and 11S fractions induced the formation of IgM and IgG antibodies. The PCA test showed that only the 7S fraction was allergenic leading to the production of IgE antibodies. Another evidence that reinforces the allergenicity of the 7S soy protein fraction is the presence of IgG1 specific antibodies reactive to this protein fraction in immunized mice. Our study shows that the 7S soy protein fraction is important to elicit allergic reactions in mice and may contribute to elucidate the allergenicity of soy-derived products.; Sabe-se que uma parte da população...

Protein fractions and In Vitro fermentation of protein feeds for ruminants

Guevara-Mesa,A. L.; Miranda-Romero,L. A.; Ramírez-Bribiesca,J. E.; González-Muñoz,S. S.; Crosby-Galvan,M. M.; Hernández-Calva,L. M.; Razo-Rodríguez,O. E. Del
Fonte: Universidad Autónoma de Yucatán, Facultad de Medicina Veterinaria Publicador: Universidad Autónoma de Yucatán, Facultad de Medicina Veterinaria
Tipo: Artigo de Revista Científica Formato: text/html
Publicado em 01/08/2011 Português
Relevância na Pesquisa
66.08%
The objective of this study was to evaluate 20 protein feeds grouped in forages, vegetal by- products and animal by-products used for ruminant diets. Protein fractions (PF): A, non-protein nitrogen (NPN); B1, buffer-soluble protein; B2, buffer-insoluble, NDF-soluble protein; B3, NDF-insoluble, ADF-soluble protein; and C, ADF-insoluble protein, were determined for each ingredient. Protein composition was correlated with total gas production in vitro (GP), gas production rate (S), lag time (L), DM disappearance (DMDIV) and residual protein (RPIV). The completely randomised designed was analysed using mixed proc. and Tukey contrasts. Forages contained 18.29, 7.86, 66.00, 2.96, 4.89% of fractions A, B1, B2, B3 and C, respectively. Vegetable byproducts contained 22.55, 4.55, 59.51, 8.84, 4.55% of each fraction, in the same order. Animal by-products contained 19.13, 4.52, 70.24, 3.74, 2.37% of each fraction, in the same order. Vetch, wheat bran and poultry litter had the greatest Vmax in each group. Vmax was correlated (P≤0.01) with total protein (r = -0.45), ADF (r = 0.27) and DMDIV (r = 0.61). In conclusion, there were differences in protein composition and kinetics of in vitro gas production among ingredients.

Changes in protein fractions, trypsin inhibitor and proteolytic activity in the cotyledons of germinating Chickpea

Neves,Valdir Augusto; Lourenço,Euclides Joaquim
Fonte: Sociedad Latinoamericana de Nutrición Publicador: Sociedad Latinoamericana de Nutrición
Tipo: Artigo de Revista Científica Formato: text/html
Publicado em 01/09/2001 Português
Relevância na Pesquisa
66.06%
The chickpea seed germination was carried out in 6 days. During the period it was observed a little variation on total nitrogen contents, however the non protein nitrogen was double. A decrease of 19.1 and 20.6% in relation to total nitrogen was observed to the total globulin and albumin fractions, respectively. The gel filtration chromatography on Sepharose CL-6B and SDS-PAGE demonstrated alterations on the distribution patterns of the albumin and total globulin fractions between the initial and the sixth day of germination suggesting the occurrence of protein degradation in the germination process.The assay for acid protease only appeared in the albumin fraction with casein and chickpea total globulin as substrates, whereas the former was more degradated than the latter, however the transformations detected in the protein fractions apppear indicated that others enzymes could be acting during the process. The trypsin inhibitor activity had a little drop after six day of germination indicating a possible increase on the digestibility of the proteins.