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Immunochemical Cross-Reactions of Human Amyloid Proteins with Human Immunoglobulin Light Polypeptide Chains¹

Laboratory of Experimental Pathology, National Institute of Arthritis and Metabolic Diseases, and the Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20014

Abstract

Antisera to three human amyloid preparations were used to study antigenic relations between seven purified amyloid fibril proteins and 49 human Bence Jones proteins. Two of the amyloid proteins were antigenically similar to each other and shared antigenic determinants with 23 of 26 kappa light polypeptide chains. The other five amyloid proteins shared antigenic determinants among themselves and with 7 of 23 lambda light polypeptide chains. There was no evidence for either the presence or absence of an amyloid-specific antigenic determinant. These immunochemical data support the concept that the amyloid fibril proteins examined derive primarily from immunoglobulin light chains.

Footnotes

¹ Presented in part at the 63rd Annual Meeting of the American Society for Clinical Investigation, Atlantic City, N. J., May 3, 1971.