Human Apolipoprotein C-II Forms Twisted Amyloid Ribbons and Closed Loops

Human apolipoprotein C-II (apoC-II) self-associates in solution to form aggregates with the characteristics of amyloid including red-green birefringence in the presence of Congo Red under cross-polarized light, increased fluorescence in the presence of thioflavin T, and a fibrous structure when exam...

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Veröffentlicht in:	Biochemistry (Easton) 2000-07, Vol.39 (28), p.8276-8283
Hauptverfasser:	Hatters, Danny M, MacPhee, Cait E, Lawrence, Lynne J, Sawyer, William H, Howlett, Geoffrey J
Format:	Artikel
Sprache:	eng
Schlagworte:	Alzheimer Disease - metabolism Amyloid - metabolism Amyloid beta-Peptides - chemistry Apolipoprotein C-II Apolipoproteins C - chemistry Apolipoproteins C - ultrastructure Chromatography, Gel Circular Dichroism Congo Red - metabolism Humans Microscopy, Electron Protein Conformation Spectrometry, Fluorescence Thiazoles - metabolism Tryptophan - chemistry Ultracentrifugation
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