Characterization of PrP binding proteins.

B Oesch

doi:10.1098/rstb.1994.0042

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Characterization of PrP binding proteins.

B Oesch

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Abstract

Prions cause spongiform degeneration in various mammalian species. The scrapie prion protein (PrPSc) is part of the infectious particle and may mediate infection and spreading of the disease in the brain. It was therefore of interest to purify and analyse PrP ligands (Plis). Plis were identified on ligand blots using either intact PrP or peptides corresponding to the central portion of PrP. Here, characterization of a 110 and a 125 kDa Pli is reported. Both Plis were found in total membrane fractions and could be extracted with carbonate indicating that they are not integral membrane proteins. On sucrose gradients both PrP ligands sedimented with high density particles.

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Animals Brain Carrier Proteins Centrifugation, Density Gradient Cricetinae Detergents Hydrogen-Ion Concentration Ligands Molecular Weight Nerve Tissue Proteins PrPSc Proteins Prion Diseases Prions Journal Article Research Support, Non-U.S. Gov't

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B Oesch. 1994-03-29. Characterization of PrP binding proteins.. https://doi.org/10.1098/rstb.1994.0042

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