Characterization of PrP binding proteins.
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.
Oesch
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Brain Research Institute, University of Zürich, Switzerland.
D000818:Animals; D001921:Brain / Q000378:metabolism; D002352:Carrier Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D002499:Centrifugation, Density Gradient; D006224:Cricetinae; D003902:Detergents; D006863:Hydrogen-Ion Concentration; D008024:Ligands; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D018620:PrPSc Proteins; D017096:Prion Diseases / Q000378:metabolism; D011328:Prions / Q000378:metabolism*
D002352:Carrier Proteins; D003902:Detergents; D008024:Ligands; D009419:Nerve Tissue Proteins; D018620:PrPSc Proteins; D011328:Prions