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The N-terminal segment of protein AA determines its fibrillogenic property.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1992 Jan 15; Vol. 182 (1), pp. 27-33. - Publication Year :
- 1992
-
Abstract
- The amyloid fibril protein AA consists of a varying long N-terminal part of the precursor protein serum AA. By using synthetic peptides corresponding to human and murine protein AA segments and cyanogen bromide fragments of human protein AA, we show evidence that the amyloidogenic part of the molecule is the first 10-15 amino acid long segment. Amino acid substitutions in this part of the molecule may explain why only one of the two mouse SAA isoforms is amyloidogenic.
- Subjects :
- Amino Acid Sequence
Amyloidosis metabolism
Amyloidosis pathology
Animals
Humans
Kidney metabolism
Kidney pathology
Mice
Microscopy, Electron
Molecular Sequence Data
Oligopeptides chemical synthesis
Serum Amyloid A Protein genetics
Serum Amyloid A Protein physiology
Serum Amyloid A Protein ultrastructure
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 182
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 1731787
- Full Text :
- https://doi.org/10.1016/s0006-291x(05)80107-x