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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
25
|
| pubmed:dateCreated |
1985-4-18
|
| pubmed:abstractText |
A major protein was identified that purifies with the scrapie agent extracted from infected hamster brains. The protein, designated PrP 27-30, was differentiated from other proteins in purified fractions containing the scrapie agent by its microheterogeneity (Mr 27000-30000) and its unusual resistance to protease digestion. PrP 27-30 was found in all fractions enriched for scrapie prions by discontinuous sucrose gradient sedimentation or sodium dodecyl sarcosinate-agarose gel electrophoresis. It is unlikely that PrP 27-30 is a pathologic product because it was found in fractions isolated from the brains of hamsters sacrificed prior to the appearance of histopathology. If PrP 27-30 is present in normal brain, its concentration must be 100-fold lower than that found in equivalent fractions from scrapie-infected hamsters. Three protease-resistant proteins similar to PrP 27-30 were found in fractions obtained by discontinuous sucrose gradient sedimentation of scrapie-infected mouse brain. These proteins were not evident in corresponding fractions prepared from normal mouse brain. One-dimensional peptide maps comparing PrP 27-30 and normal hamster brain proteins of similar molecular weight demonstrated that PrP 27-30 has a primary structure which is distinct from these normal proteins. Heating substantially purified scrapie fractions to 100 degrees C in sodium dodecyl sulfate inactivated the prion and rendered PrP 27-30 susceptible to protease digestion. Though the scrapie agent appears to be hydrophobic, PrP 27-30 remained in the aqueous phase after extraction with organic solvents, indicating that it is probably not a proteolipid. PrP 27-30 is the first structural component of the scrapie prion to be identified.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Prions,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/glutamyl endopeptidase
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0006-2960
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
4
|
| pubmed:volume |
23
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
5898-906
|
| pubmed:dateRevised |
2008-11-21
|
| pubmed:meshHeading |
pubmed-meshheading:6395885-Animals,
pubmed-meshheading:6395885-Brain Chemistry,
pubmed-meshheading:6395885-Centrifugation, Density Gradient,
pubmed-meshheading:6395885-Cricetinae,
pubmed-meshheading:6395885-Electrophoresis, Agar Gel,
pubmed-meshheading:6395885-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6395885-Endopeptidases,
pubmed-meshheading:6395885-Hot Temperature,
pubmed-meshheading:6395885-Mice,
pubmed-meshheading:6395885-Molecular Weight,
pubmed-meshheading:6395885-Nerve Tissue Proteins,
pubmed-meshheading:6395885-Peptide Fragments,
pubmed-meshheading:6395885-Peptide Hydrolases,
pubmed-meshheading:6395885-Prions,
pubmed-meshheading:6395885-Protein Denaturation,
pubmed-meshheading:6395885-Scrapie,
pubmed-meshheading:6395885-Serine Endopeptidases,
pubmed-meshheading:6395885-Sheep,
pubmed-meshheading:6395885-Time Factors,
pubmed-meshheading:6395885-Viral Proteins
|
| pubmed:year |
1984
|
| pubmed:articleTitle |
Molecular characteristics of the major scrapie prion protein.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|