English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Previous studies have shown that the N ε -carboxymethyl group is linked to not only one or more N-terminal Lys residues but also to one or more Lys residues of the protease-resistant core region of the pathogenic prion isoform (PrP Sc ) in prion-infected brains. Using an anti-advanced glycation end product (AGE) antibody, we detected nonenzymatically glycated PrP Sc  (AGE-PrP Sc ) in prion-infected brains following concentration by a series of ultracentrifugation steps with a sucrose cushion. In the present study, the levels of  in vitro  nonenzymatic glycation of PrP Sc  using sucrose were investigated to determine whether sucrose cushion can artificially and nonenzymatically induce  in vitro  glycation during ultracentrifugation. The first insoluble pellet fraction following the first ultracentrifugation (PU 1st ) collected from 263K scrapie-infected brains was incubated with sucrose, glucose or colloidal silica coated with polyvinylpyrrolidone (percoll). None of the compounds  in vitro  resulted in AGE-PrP Sc . Nonetheless, glucose and percoll produced AGEs  in vitro  from other proteins within PU 1st  of the infected brains. This reaction could lead to the AGE-modified polymer(s) of nonenzymatic glycation-prone protein(s). This study showed that PrP Sc  is not nonenzymatically glycated  in vitro  with sucrose, glucose or percoll and that AGE-modified PrP Sc  can be isolated and enriched from prion-infected brains.

biological chemistry

Semi-purification procedures of prions from a prion-infected brain using sucrose has no influence on the nonenzymatic glycation of the disease-associated prion isoform