Isolation and characterization of native soluble and membrane bound prion proteins from calf brain

The prion protein is the unique infectious agent that lacks nucleic acids. It exists in two isoforms, the cellular protein and the pathogenic form, which have the same amminoacidic sequence but different secondary and tertiary structures. This thesis work show the obtained results in the attempt to optimize a methodological approaches for isolation and characterization of the membrane bound PrPC from bovine brain in its complete molecular organization which includes polypeptide, glucidic and phosphatidyl inositol moieties (membrane PrPC) . The study extended to a cytosolic form of PrPC (soluble PrPC) revealed to be highly represented in the bovine brain. The presence of PrPC was revealed in the different phases of the study by the immunological techniques of Western blot and Elisa