To build a new research model of the bovine prion protein (PrP), we cloned and expressed a truncated fragment of the PrP and explore its functional feature. We obtained a recombinant protein of the PrP fragment (90 ∼231 amino acid). We analyzed the proteinase K resistance by enzymolysis, the binding force of the recombinant protein and bacteriophage Ff gene 5 protein (G5P) by affinity chromatography, and the enrichment effect of G5P on the recombinant PrP by Western blot. The recombinant protein was fully hydrolyzed by proteinase K. It specifically binds with G5P and the detectability limi...
