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

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Abstract
A monclonal immunoglobulin has been isolated from the peritoneal fluid of a patient with primary am yloidosis. 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 resi dues and were typical of a k I light chain. Molecular Weight studies suggested that the fibril protein was com posed 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.