149 resultados para Proteína C-reativa


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504 (five hundred four) 1 day old male chicks from a commercial broiler line (Ag Ross 308) were used, distributed in 12 treatments, with 6 replicates per treatment. The experimental design was casually blocked and treatments were organized in a 2x2x3 factorial arrangement: two available phosphorus levels (0.45 and 0.34%), two phytase inclusion levels (0 and 1200 FTU/kg) and three crude protein levels (22.5; 20.5 and 18.5%). Tibia calcium percentage was influenced by protein and phosphorus levels in the diet, when using phytase. Tibia ash levels showed a linear effect when enzymes were added and showed a quadractic effect without it, and the higher value was observed with 22.5% crude protein in the diet. With higher phosphorus levels a linear effect was observed between crude protein in the diet and tibia ash weights, as a higher protein level had lower tíbia ash weight.

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The experiment was conducted to evaluate the ingestive behavior of feedlot lambs fed with an exclusive diet of concentrate with different percentages of protein (14, 16, 18, and 20%). A total of twenty four Santa Inês crossbred lambs, not castrated, with approximately 180 days of age, average live weight of 25kg, confined, in a completely randomized design, with four treatments and six repetitions. The time spent on feeding decreased linearly in 0.20 hours/day for each 1% increasing in protein percentage in the diet, the idleness increased linearly in 0.25 hours/day, and the total chewing decreased linearly in 0.25 hours/day. The increase in the protein percentage in the diet increased the feed efficiency linearly (kg DM and NDF/hour) in 0.038 and 0.005kg/hour, respectively, for DM and NDF fractions. However, the intake of dry matter (DM) and neutral detergent fiber (NDF), the rumination efficiency (kg DM and NDF/hour), as well as the period (nº /day) and the time (min) spent on feeding, ruminating and idling were not influenced by different protein percentages in the diet.

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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As proteínas da família TRF2 (“TTAGGG repeat-binding factor 2”) fazem parte de complexos multiprotéicos responsáveis pela manutenção dos telômeros de alguns eucariotos. Elas apresentam domínios funcionais que a caracterizam como proteínas que interagem com DNA telomérico na forma de dupla fita. São eles, o domínio de interação com o DNA do tipo Myb-like, localizado na porção C-terminal, um domínio acídico N-terminal e um domínio de homodimerização TRFH (“TRF homology domain for homodimerization”). A proteína TRF2 também está envolvida na formação de estruturas teloméricas terminais denominadas “t-loops”. O intuito deste projeto é a clonagem, expressão em vetor bacteriano (pMAL) e a purificação de uma proteína homóloga as proteínas teloméricas TRFs humana em parasitas do gênero Leishmania, especificamente a espécie Leishmania amazonensis (LaTRF). Primeiramente foram desenhados iniciadores (primers) utilizados para a amplificação da sequência LaTRF por PCR. O(s) produto(s) de amplificação foram clonados em vetores de clonagem para produtos de PCR e sequenciados para análise. Uma vez obtida a seqüência da LaTRF, o inserto contendo o gene foi subclonado direcionalmente e na mesma fase de leitura do vetor de expressão bacteriano (pMAL-c5x, NEB) para obtenção e futura purificação da proteína recombinante. Verificou-se a expressão da proteína recombinante LaTRF utilizando SDS-PAGE e “Western Blot”. Pelos resultados obtidos na análise de expressão em pequena escala da proteína recombinante, foi observado possíveis indícios de que esta esteja sendo expressa. Com isso, torna-se possível a tentativa de uma expressão em grande escala utilizando esse mesmo sistema bacteriano (pMAL) a fim de se obter a proteína purificada que poderá ser futuramente utilizada para ensaios de “pull-down” dentre outras aplicações

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Kaposi´s sarcoma associated herpesvirus (KSHV) or human herpesvirus 8 (HHV-8) is a gammaherpesvirus essential for the development of all forms of Kaposi´s sarcoma (KS). The KSHV’s life cycle is basically divided into latent and lytic phases, which have distinct viral gene expression profiles. Some important oncogenic products of KSHV are expressed during the lytic phase, including the viral K1 protein. As an effect of interfer-ence with intracellular signaling, K1 expression increases proliferation and survival of KSHV-infected cells. Due to its high level of genetic variability compared to other re-gions of the viral genome, the K1-encoding ORF (ORF-K1) is commonly evaluated for KSHV genotyping. It remains unclear whether different viral genotypes have particular biological effects that might modify the KSHV oncogenicity. The present study aimed to contribute to the establishment of an experimental in vitro model for evaluation of the K1 protein from common KSHV genotypes. Recombinant expression vectors with the ORF-K1 from KSHV genotypes A, B and C were prepared by genetic cloning. The recombi-nant vectors pKSHVOK1 obtained by cloning were sequenced for structural validation. After that, HEK293 cell line was transfected with the recombinant vectors, and proteins were extracted for expression analysis by Western blot technique, for K1 functional vali-dation. Results showed that ORF-K1 vectors containing KSHV ORF-K1 from the A, B and C genotypes were produced and structurally validated by DNA sequencing. The K1 expression at the protein level was also confirmed by immunoblots using an antibody for FLAG detection, an epitope from the vector that binds to K1. Based on presented re-sults, it´s possible to conclude that the recombinant vectors will be able to be used in future studies of K1 protein biological properties from distinct KSHV genotypes

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)

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Pós-graduação em Biotecnologia - IQ

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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)

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Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)