Indentity of a peritoneal fluid immunoglobulin light chain and the amyloid fibril i primary amyloidosis

Paul J. Block, Martha Skinner, Merrill D. Benson, Alan S, Cohen

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

A monoclonal immunoglobulin has been isolated from the peritoneal fluid of a patient with primary amyloidosis. The immunoglobulin was reduced and alkylated and the light and heavy chains were compared to the major protein constituent of that patient's hepatic amyloid fibrils. N-terminal amino acid sequences of the light chain and amyloid fibril were identical when carried to 20 residues and were typical of a kappa I light chain. Molecular weight studies suggested that the fibril protein was composed of an intact light chain with a molecular weight of 23,000. The hypothesis that amyloid fibril protein in primary amyloid is derived from circulating monoclonal immunoglobulin is discussed.

Original languageEnglish (US)
Pages (from-to)755-759
Number of pages5
JournalArthritis & Rheumatism
Volume19
Issue number4
DOIs
StatePublished - Jan 1 1976
Externally publishedYes

ASJC Scopus subject areas

  • Immunology and Allergy
  • Rheumatology
  • Immunology
  • Pharmacology (medical)

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