CHARACTERIZATION OF PRP BINDING-PROTEINS

被引：8

作者：

OESCH, B

机构：

[1] Brain Research Institute, University of Zürich

来源：

PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES | 1994年 / 343卷 / 1306期

关键词：

D O I：

10.1098/rstb.1994.0042

中图分类号：

Q [生物科学];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

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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页码：443 / 445

页数：3

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