The complete mature bovine prion protein highly expressed in Escherichia coli: biochemical and structural studies

According to the 'protein only' hypothesis, modification of the 3-dimensional fold of the constituent cellular protein, PrPC, into the disease-associated isoform, PrPSc, is the cause of neurodegenerative diseases in animals and humans, Here we describe the high-level synthesis in Escherichia coli, and purification in the monomeric form, of a histidine-tagged full-length mature PrP (25-249) of bovine brain, termed His-PrP, Based on biochemical and spectroscopic data, His-PrP displays characteristics expected for the PrPC isoform, The reported expression system should allow the production of quantities of bovine PrPC sufficient to permit 3-dimensional structure determinations. (C) 1997 Federation of European Biochemical Societies.