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Isolation and identification by sequence analysis of experimentally induced guinea pig amyloid fibrils.

Authors
  • Skinner, M
  • Cathcart, E S
  • Cohen, A S
  • Benson, M D
Type
Published Article
Journal
The Journal of experimental medicine
Publication Date
Sep 01, 1974
Volume
140
Issue
3
Pages
871–876
Identifiers
PMID: 4213201
Source
Medline
License
Unknown

Abstract

Amyloidosis was produced experimentally in guinea pigs by multiple casein injections. Amyloid fibrils were isolated and fractionated and a protein obtained that had an amino acid composition comparable with A protein, a unique nonimmunoglobulin constituent of secondary amyloid deposits. N-terminal sequence analysis demonstrated a sequence homologous with that of A proteins from human and monkey preparations but preceded by a 5-residue peptide which had an N-terminal histidine. A definite species specificity in A protein from human and guinea pig was identified on immunologic analysis.

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