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. 1974 Sep 1;140(3):871–876. doi: 10.1084/jem.140.3.871

ISOLATION AND IDENTIFICATION BY SEQUENCE ANALYSIS OF EXPERIMENTALLY INDUCED GUINEA PIG AMYLOID FIBRILS

Martha Skinner 1, Edgar S Cathcart 1, Alan S Cohen 1, Merrill D Benson 1
PMCID: PMC2139617  PMID: 4213201

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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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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