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

M. Skinner, E. S. Cathcart, A. S. Cohen, Merrill Benson

Research output: Contribution to journalArticle

40 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)871-876
Number of pages6
JournalJournal of Experimental Medicine
Volume140
Issue number3
StatePublished - 1974
Externally publishedYes

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Amyloid
Sequence Analysis
Guinea Pigs
Proteins
Species Specificity
Amyloid Plaques
Amyloidosis
Sequence Homology
Caseins
Histidine
Haplorhini
Amino Acids
Peptides
Injections

ASJC Scopus subject areas

  • Immunology

Cite this

Isolation and identification by sequence analysis of experimentally induced guinea pig amyloid fibrils. / Skinner, M.; Cathcart, E. S.; Cohen, A. S.; Benson, Merrill.

In: Journal of Experimental Medicine, Vol. 140, No. 3, 1974, p. 871-876.

Research output: Contribution to journalArticle

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