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KMID : 1023520050280040393
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Korean Journal of Veterinary Service
2005 Volume.28 No. 4 p.393 ~ p.405
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Generation of ovine recombinant prion protein (25-232): Characterisation via anti-PrP monoclonal antibodies and CD spectroscopy
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Yang Su-Jeong
Thackray Alana
Bujdoso Raymond
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Abstract
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In prion pathogenesis, the structural conversion of the cellular prion protein to its abnormal isomer 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 presents lower convertibility to than wild type 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 . These variants showed similar immunoreactivity against anti-PrP monoclonal antibodies in Western blot and ELISA. The refolded and presented the secondary structural content to similar extent via CD spectroscopy analysis. The inherited structural features of and under the different biophysical conditions are in the middle of investigation.
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KEYWORD
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Ovine PrP, Polymorphism, Recombinant PrP
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