Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein.
Proc Natl Acad Sci U S A
; 83(8): 2662-6, 1986 Apr.
Article
en En
| MEDLINE
| ID: mdl-3458224
ABSTRACT
Isolation of Alzheimer disease amyloid plaque core protein (APCP) was carried out by repetitive NaDodSO4/EDTA/sucrose extractions and by Ficoll-400 density-gradient centrifugations. The enriched APCP-Ficoll interface was labeled with the fluorochrome thioflavin T and separated from the contaminating lipofuscin by fluorescence-activated cell sorting. Electron microscopy demonstrated that APCP is made of two different kinds of filaments measuring 5.5-6 nm and 10-12 nm, respectively, and of variable length. Purified APCP and lipofuscin were chemically modified by performic acid oxidation. The amino acid composition of APCP revealed a high content of glycine and valine (30%) and 1% cysteine. By contrast, the protein moiety of the copurified lipofuscin contained 16% cysteine. The amino acid composition of APCP did not resemble that of any known protein.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Química Encefálica
/
Enfermedad de Alzheimer
/
Amiloide
/
Proteínas del Tejido Nervioso
Límite:
Humans
Idioma:
En
Revista:
Proc Natl Acad Sci U S A
Año:
1986
Tipo del documento:
Article