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Scrapie-infected cells, isolated prions, and recombinant prion protein: A comparative study
- Source :
- Biopolymers. 74:163-167
- Publication Year :
- 2004
- Publisher :
- Wiley, 2004.
-
Abstract
- Fourier -transform infrared microscopic spectra of scrapie-infected nervous tissue measured at high spatial resolution (approximately 6 microm) were compared with those obtained from the purified, partly proteinase K digested scrapie isoform of the prion protein isolated from nervous tissue of hamsters infected with the same scrapie strain (263K) to elucidate similarities/dissimilarities between prion structure investigated in situ and ex vivo. A further comparison is drawn to the recombinant Syrian hamster prion protein SHaPrP(90-232) after in vitro conformational transition from the predominantly alpha-helical isoform to beta-sheet-rich structures. It is shown that prion protein structure can be investigated within tissue and that detectability of regions with elevated beta-sheet content as observed in microspectra of prion-infected tissue strongly depends on spatial resolution of the experiment.
- Subjects :
- Gene isoform
Prions
Protein Conformation
Biophysics
Hamster
Scrapie
In Vitro Techniques
Biochemistry
Protein Structure, Secondary
Prion Diseases
law.invention
Biomaterials
Protein structure
law
Cricetinae
Ganglia, Spinal
Spectroscopy, Fourier Transform Infrared
medicine
Animals
Protein Isoforms
Mesocricetus
biology
Chemistry
Nervous tissue
Organic Chemistry
General Medicine
biology.organism_classification
Proteinase K
Virology
Molecular biology
Recombinant Proteins
medicine.anatomical_structure
biology.protein
Recombinant DNA
Endopeptidase K
Subjects
Details
- ISSN :
- 10970282 and 00063525
- Volume :
- 74
- Database :
- OpenAIRE
- Journal :
- Biopolymers
- Accession number :
- edsair.doi.dedup.....2cae3cafe1a44dfcc7be34d867d18bd6