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Copper Binding to the PrP Isoforms: a Putative Marker of Their Conformation and Function
- Publication Year :
- 2001
- Publisher :
- American Society for Microbiology, 2001.
-
Abstract
- We show here that PrPC, the normal isoform of the prion protein (PrPSc), could be retained by a Cu2+-loaded resin through two different binding sites. Contrarily, PrPScwas not retained at all by such resin. This constitutes a new prion-specific property of PrPSc, which in addition to protease resistance and β-sheet content, may result from its aberrant conformation.
- Subjects :
- Gene isoform
PrPSc Proteins
Protein Conformation
medicine.medical_treatment
animal diseases
Immunology
Biology
Microbiology
Chromatography, Affinity
Protein structure
Copper binding
Virology
Cricetinae
medicine
Animals
Protein Isoforms
PrPC Proteins
Prion protein
Binding site
Protease
Molecular biology
nervous system diseases
Biochemistry
nervous system
Insect Science
Pathogenesis and Immunity
Function (biology)
Copper
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Accession number :
- edsair.doi.dedup.....84422bc1e1c935c09ee4b4a791a5e521