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Flavonoids Modulate the Proliferation of Neospora caninum in Glial Cell Primary Cultures
Rosan Barbosa de Matos,Suzana Braga-de-Souza,Bruno Pena Seara Pitanga,Victor Diogenes Amaral da Silv,Erica Etelvina Viana de Jesus,Alexandre Morales Pinheiro,Maria de Fatima Dias Costa,Ramon dos Santo 대한기생충학열대의학회 2014 The Korean Journal of Parasitology Vol.52 No.6
C.F. Rosaneli,A.E. Bighetti,M.A. Antonio,J.E. Carvalho,V.C. Sgarbieri 한국식품영양과학회 2004 Journal of medicinal food Vol.7 No.3
The protective effect of a whey protein concentrate (WPC) was studied in three models of stomach ulcerative lesions induction: subcutaneous injection of indomethacin, and stress induced by either intraperitoneal injection of reserpine, or immobilization and holding in the cold (4 degrees C, 2 hours). Adult Wistar rats (300-400 g) were used for acute (single-dose), repetitive, or subchronic (10 days) administration of WPC prior to treatment with the ulcerogenic factors. The best protection was achieved in the indomethacin model for repetitive and subchronic experiments, reaching 50.1% and 44%, respectively, inhibition of the ulcerative lesions, which was significant at 1% probability (P <.01). For the immobilization and cold model, maximum inhibition by WPC was 22.1%, and that for the reserpine model was 23.8%. In both models the inhibition was not significant (P >.05) compared with saline (negative control).
( Karla Silva Teixeira Souza ),( Rosane Freitas Schwan ),( Disney Ribeiro Dias ) 한국미생물 · 생명공학회 2014 Journal of microbiology and biotechnology Vol.24 No.4
In this study, crude glycerol was used as a carbon source in the cultivation of wild yeasts, aiming at the production of microbial lipids and citric acid. Forty yeasts of different sources were tested concerning their growth in crude and commercial glycerol. Four yeasts (Lindnera saturnus UFLA CES-Y677, Yarrowia lipolytica UFLA CM-Y9.4, Rhodotorula glutinis NCYC 2439, and Cryptococcus curvatus NCYC 476) were then selected owing to their ability to grow in pure (OD600 2.133, 1.633, 2.055, and 2.049, respectively) and crude (OD600 2.354, 1.753, 2.316, and 2.281, respectively) glycerol (10%, 20%, and 30%). Y. lipolytica UFLA CM-Y9.4 was selected for its ability to maintain cell viability in concentrations of 30% of crude glycerol, and high glycerol intake (18.907 g/l). This yeast was submitted to lipid production in 30 g/l of crude glycerol, and therefore obtained 63.4% of microbial lipids. In the fatty acid profile, there was a predominance of stearic (C18:0) and palmitic (C16:0) acids in the concentrations of 87.64% and 74.67%, respectively. We also performed optimization of the parameters for the production of citric acid, which yielded a production of 0.19 g/l of citric acid in optimum conditions (38.4 g/l of crude glycerol, agitation of 184 rpm, and temperature of 30oC). Yarrowia lipolytica UFLA CM-Y9.4 presented good lipid production when in the concentration of 30 g/l of glycerol. These data may be used for production in large quantities for the application of industrial biodiesel.
Correia, F.F.,Waterbury, T.L.,Rosan, B.,DiRienzo, J.M. Korean Academy of Oral Biology and the UCLA Dental 2001 International Journal of Oral Biology Vol.26 No.1
The major outer membrane porin, FomA, from Fusobacterium mucleatum ATCC 10953 was previously shown to be a coaggregation receptor for Streptococcus crista CC5A. The fomA gene was amplified by PCR and cloned in Escherichia coli. The nucleotide sequence of the recombinant gene contained a three base pair deletion and four single base differences compared to the native fomA sequence. The recombinant gene product was glutathione-S-transferase (GST). The GST portion was removed by treatment with thrombin and the FomA portion purified in milligram quantities. The purified recombinant protein contained a glycylserine dipeptide at its amino terminus, bound IgG from antiserum made against native FomA, and retained the heat-modifiable property of the native protein. However, the recombinant FomA failed to bind to S. crista CC5A or inhibit coaggregation between this bacterium and F. nucleatum. FomA may require outer membrane components, such as lipopolysaccharide, to stabilize the protein in a structure recognized by the streptococcal adhesin.