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

J Exp Med. 1974 Sep 1;140(3):871-6. doi: 10.1084/jem.140.3.871.

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.

MeSH terms

  • Amino Acid Sequence
  • Amyloid / analysis*
  • Amyloid / isolation & purification
  • Amyloidosis / chemically induced
  • Amyloidosis / metabolism*
  • Animals
  • Caseins
  • Guinea Pigs
  • Immunoassay
  • Immunodiffusion
  • Precipitin Tests
  • Spleen / analysis

Substances

  • Amyloid
  • Caseins