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- Luo, Minhua, et al. Show all 8 Authors
- Biochemical and biophysical research communications 2019 v.509 no.2 pp. 570-576
- PrPSc proteins; brain; dimerization; disulfide bonds; histidine; humans; patients; scrapie
- ... The conversion of the normal prion protein (PrP) into a scrapie prion (PrPSc) is incompletely understood. Theoretically, the smallest PrP aggregate is a dimer. Human PrP contains two cysteines at positions 179 (C179) and 214 (C214) enabling disulfide bonding. Here, we report that our recombinant human PrP (r-hPrP) preparations contain 0.2–0.8% dimer, which is linked by either one or two disulfide ...