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- 저자 : Thackray, Alana (검색결과 2 건)
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Yang, Su-Jeong,Thackray, Alana,Bujdoso, Raymond The Korean Society of Veterinary Service 2005 韓國家畜衛生學會誌 Vol.28 No.4
In prion pathogenesis, the structural conversion of the cellular prion protein $(PrP^c)$ to its abnormal isomer $(PrP^{Sc})$ is believed to be a major event. The susceptibility or resistance to natural sheep scrapie is associated with polymorphisms of host PrP gene (PRNP) at amino acid residues 136, to a lesser extent 154. The 112 residue in ovine PrP displays a natural polymorphism, Methionine to Threonine, which has not been thoroughly investigated. However the cell-free conversion assay showed that ARQ with Thr112 $(T_{112}ARQ)^{1)}$ presents lower convertibility to $PrP^{Sc}$than wild type ARQ $(M_{112}ARQ)$ [1] In this study we generated ovine recombinant PrPs of 112 allelic variants by metal chelate affinity chromatography and cation exchange chromatography. The final purity of the ovine PrP ARQ was more than $95\%$. These variants showed similar immunoreactivity against anti-PrP monoclonal antibodies in Western blot and ELISA. The refolded $M_{112}ARQ$ and $M_{112}ARQ$ presented the secondary structural content to similar extent via CD spectroscopy analysis. The inherited structural features of $M_{112}ARQ$ and $M_{112}ARQ$ under the different biophysical conditions are in the middle of investigation.
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( Su Jeong Yang ),( Alana Thackray ),( Raymond Bujdoso ) 한국가축위생학회 2005 韓國家畜衛生學會誌 Vol.28 No.4
In prion pathogenesis, the structural conversion of the cellular prion protein(PrPC) to its abnormal isomer(PrPSc) is believed to be a major event. The susceptibility or resistance to natural sheep scrapie is associated with polymorphisms of host PrP gene (PRNP) at amino acid residues 136, to a lesser extent 154. The 112 residue in ovine PrP displays a natural polymorphism, Methionine to Threonine, which has not been thoroughly investigated. However the cell-free conversion assay showed that ARQ with Thr112(T112ARQ)1) presents lower convertibility to PrPSc than wild type ARQ (M112ARQ) [1]. In this study we generated ovine recombinant PrPs of 112 allelic variants by metal chelate affinity chromatography and cation exchange chromatography. The final purity of the ovine PrP ARQ was more than 95%. These variants showed similar immunoreactivity against anti-PrP monoclonal antibodies in Western blot and ELISA. The refolded M112ARQ and T112ARQ presented the secondary structural content to similar extent via CD spectroscopy analysis. The inherited structural features of M112ARQ and T112ARQ under the different biophysical conditions are in the middle of investigation.
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