Identity of a peritoneal fluid immunoglobulin light chain and the amyloid fibril in primary amyloidosis.

P. J. Block, M. Skinner, Merrill Benson, A. S. Cohen

Research output: Contribution to journalArticle

10 Citations (Scopus)

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
Pages (from-to)755-759
Number of pages5
JournalArthritis and Rheumatism
Volume19
Issue number4
StatePublished - Jul 1976
Externally publishedYes

Fingerprint

Immunoglobulin Light Chains
Ascitic Fluid
Amyloid
Light
Immunoglobulins
Molecular Weight
Amyloidogenic Proteins
Amino Acid Sequence
Proteins
Primary amyloidosis
Liver

ASJC Scopus subject areas

  • Immunology
  • Rheumatology

Cite this

Identity of a peritoneal fluid immunoglobulin light chain and the amyloid fibril in primary amyloidosis. / Block, P. J.; Skinner, M.; Benson, Merrill; Cohen, A. S.

In: Arthritis and Rheumatism, Vol. 19, No. 4, 07.1976, p. 755-759.

Research output: Contribution to journalArticle

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