Tesi etd-05152007-172801 |
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Tipo di tesi
Tesi di dottorato di ricerca
Autore
Gorini, Francesca
URN
etd-05152007-172801
Titolo
Isolation and characterization of native soluble and membrane bound prion proteins from calf brain
Settore scientifico disciplinare
BIO/10
Corso di studi
BIOTECNOLOGIE MOLECOLARI
Relatori
Relatore Prof. Mura, Umberto
Relatore Prof. Galleschi, Luciano
Relatore Prof. Paolicchi, Aldo
Relatore Prof. Galleschi, Luciano
Relatore Prof. Paolicchi, Aldo
Parole chiave
- Prion
Data inizio appello
16/03/2007
Consultabilità
Non consultabile
Data di rilascio
16/03/2047
Riassunto
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
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
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