HETEROGENEITY OF L-CHAIN SITES ON BENCE-JONES PROTEINS REACTING WITH ANTI-γ-GLOBULIN FACTORS

Abstract

Bence-Jones proteins providing a source of individual light chains were isolated from the urines of patients with multiple myeloma. Reactivity with light chains of various anti- [gamma] -globulin factors occurring in the serum of patients with rheumatoid arthritis was studied by the use of individual Bence-Jones proteins tanned to cells. The variety of patterns of reaction between rheumatoid arthritis sera and individual L-chains tanned to cells did not correlate with either the Group I or II determinants or Inv (a) typing of the Bence-Jones proteins; however, evidence for common determinants on several light-chain preparations reacting with various anti-[gamma] -globulin factors was obtained by mutual inhibition experiments as well as by identical patterns of agglutination of two Bence-Jones preparations by only 5 of the 15 agglutinating sera tested. Heterogeneous sites on L-chains appear to react with selected rheumatoid factors.