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.
ISOLATION AND IDENTIFICATION BY SEQUENCE ANALYSIS OF EXPERIMENTALLY INDUCED GUINEA PIG AMYLOID FIBRILS
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Martha Skinner, Edgar S. Cathcart, Alan S. Cohen, Merrill D. Benson; ISOLATION AND IDENTIFICATION BY SEQUENCE ANALYSIS OF EXPERIMENTALLY INDUCED GUINEA PIG AMYLOID FIBRILS . J Exp Med 1 September 1974; 140 (3): 871–876. doi: https://doi.org/10.1084/jem.140.3.871
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