RESUMEN
This paper presents, from the perspective of technological development and production, the results of an investigation examining 61 clinical studies with vaccines conducted in Brazil between 1938-2013, with the participation of the Oswaldo Cruz Institute (IOC) and the Oswaldo Cruz Foundation (Fiocruz). These studies have been identified and reviewed according to criteria, such as the kind of vaccine (viral, bacterial, parasitic), their rationale, design and methodological strategies. The results indicate that IOC and Fiocruz have accumulated along this time significant knowledge and experience for the performance of studies in all clinical phases and are prepared for the development of new vaccines products and processes. We recommend national policy strategies to overcome existing regulatory and financing constraints.
Asunto(s)
Animales , Alimentación Animal/efectos adversos , Proteínas en la Dieta/química , Modelos Biológicos , Proantocianidinas/química , Rumen/metabolismo , Brassica rapa/química , Precipitación Química , Proteínas en la Dieta/metabolismo , Fermentación , Fabaceae/efectos adversos , Fabaceae/química , Frutas/efectos adversos , Frutas/química , Estructura Molecular , Peso Molecular , Concentración Osmolar , Proteínas de Plantas/química , Proteínas de Plantas/metabolismo , Proantocianidinas/efectos adversos , Proantocianidinas/metabolismo , Rumiantes , Ribulosa-Bifosfato Carboxilasa/química , Ribulosa-Bifosfato Carboxilasa/metabolismo , Rumen/microbiología , Solubilidad , Estereoisomerismo , Albúmina Sérica Bovina/química , Albúmina Sérica Bovina/metabolismoRESUMEN
Ribulose-1,5-bisphosphate carboxylase has been isolated from a synthetic cereal triticale and purified using a newly developed rapid procedure involving precipitation with ammonium sulphate (35-55% saturation), DEAE-cellulose (DE-52) chromatography and filtration through Sepharose CL-68. Molecular weights of the enzyme subunits are 15.5 and 52 kDa which corresponds to 540 kDa for the hexadecameric holoenzyme. Isoelectric focussing showed that the enzyme has a pI of 4.2. Various kinetic constants determined under aerobic conditions are: Km (CO2), 118 microM; Km (RuBP), 220 microM (at 20 mM NaHCO3) and Vmax, 690 nmole CO2 fixed/mg enzyme/min.