Article
Prion proteins with insertion mutations have altered N-terminal conformation and increased ligand binding activity and are more susceptible to oxidative attack.
The Journal of biological chemistry - 21 Apr 2006
Yin Shaoman, Yu Shuiliang, Li Chaoyang, Wong Poki, Chang Binggong, Xiao Fan, Kang Shin-Chung, Yan Huimin, Xiao Gengfu, Grassi Jacques, Tien Po, Sy Man-Sun
Abstract excerpt
We compared the biochemical properties of a wild type recombinant normal human cellular prion protein, rPrP(c), with a recombinant mutant human prion protein that has three additional octapeptide repeats, rPrP(8OR). Monoclonal antibodies that are specific for the N terminus of rPrP(c) react much better with rPrP(8OR) than rPrP(c), suggesting that the N terminus of rPrP(8OR) is more exposed and hence more...
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