The Journal of Experimental Medicine
VeriKine-HS Human IFN-Beta
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The Journal of Experimental Medicine, Vol 140, 871-876, Copyright © 1974 by The Rockefeller University Press

BRIEF DEFINITIVE REPORTS

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

Martha Skinner 1, Edgar S. Cathcart 1, Alan S. Cohen 1, and Merrill D. Benson 1

1 From the Arthritis and Connective Tissue Disease Section, Evans Department of Clinical Research, University Hospital, and the Thorndike Memorial Laboratory and Division of Medicine, Boston City Hospital, Boston, Massachusetts 02118

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.

Submitted on May 20, 1974


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