Two myeloma globulins, IgG1-kappa and IgG1-lambda, from a single patient (Im). I. Purification and immunochemical characterization.

Abstract

Electrophoretic analysis of the serum from a patient Im suffering from a multiple myeloma revealed the existence of two abnormal bands. Purification of these two fractions on a DEAE—cellulose column showed that both fractions had the same sedimentation coefficient (7S), belonged to the same class (IgG), and subclass (γl) and bore the same allotype (Gm(1)). However, the heavy (H) chains of one immunoglobulin were associated with type κ light (L) chains whereas those of the other were associated with type λ L chains. Three individual antigenic determinants were found in these two proteins. One was common to the H chains of both proteins and the other two were each specific to one of the L chains. These results suggest that the myeloma cells of patient (Im) were able to produce at least three polypeptide chains, one H chain and two different types of L chains.