Clusterin Prevents Aggregation of Neuropeptide 106-126 in Vitro
| Autor: | N Edington, S McHattie |
|---|---|
| Rok vydání: | 1999 |
| Předmět: |
Amyloid
Prions Molecular Sequence Data Biophysics Neuropeptide In Vitro Techniques Biochemistry Antibodies Animals Amino Acid Sequence Molecular Biology Peptide sequence Glycoproteins chemistry.chemical_classification biology Clusterin Neuropeptides Cell Biology Molecular biology Peptide Fragments eye diseases In vitro Encephalopathy Bovine Spongiform Microscopy Electron chemistry biology.protein sense organs Antibody Glycoprotein Molecular Chaperones |
| Zdroj: | Biochemical and Biophysical Research Communications. 259:336-340 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1999.0781 |
| Popis: | The prion/amyloid neuropeptide 106-126 spontaneously aggregates to form fibrillar structures in vitro. The aggregation in vitro could be prevented in a dose-related manner by clusterin, and the specificity of this action was confirmed by reversal with antibody to clusterin. The relevance of these observations is discussed in relation to previous observations that clusterin and PrPBSE colocalise in naturally occurring cases of BSE. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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