With the aim to follow large scale production of recombinant E rns from Classical Swine Fever Virus, a monoclonal specific antibody was obtained and optimized it downstream lab scale purification. The anti-E rns gamma globulins were purified through Protein A and Protein G affinity chromatography from ascites fluid. Three binding factors were assessed (pH, flow rate and buffer) to define dynamic binding capacity. The best binding condition to Protein A (6.6 mg/mL of matrix) was in phosphate buffer, pH 8.0 and linear flow rate of 78cm/h with a purity of 90 %. For Protein G, the best arrangement of factors was phosphate buffer, pH 7.0 and linear flow 178cm/h with 6.45mg/mL of adsorbed antibody with a purity of 95 %. The nProtein-A Sepharose matrix allowed 1.21 times more recovery than the nProtein-G Sepharose matrix. However, the elutions obtained with the G-protein were more pure.

<p>Se analizó la expresión constitutiva del gen reportero de la ß-Glucuronidasa (GUS) fusionado a tres promotores: el 35S del virus del mosaico de la coliflor (CaMV), el promotor quimérico A9 que contiene la actina-1 de arroz y el promotor ubiquitina-1 de maíz. La actividad de los promotores fue analizada cualitativa y cuantitativamente en diferentes tejidos y estadíos de crecimiento de plantas de arroz (variedad J-104) transformadas mediante biobalística. Se demostró la expresión constitutiva de GUS bajo los promotores estudiados, con distintos patrones de actividad relativa en hojas, tallos y raíces de plantas in vitro y ex vitro, y en plantas de la progenie T 1. Bajo el promotor quimérico A9 se lograron los mayores niveles de expresión GUS en todos los tejidos y fases de crecimiento de las plantas.</p>

No abstract