SIMILARITIES IN THE LIGHT CHAINS OF ANTI-γ-GLOBULINS SHOWING CROSS-IDIOTYPIC SPECIFICITIES

Abstract

A marked homogeneity of the light chains was observed in an analysis of 17 IgM proteins with anti-γ-globulin activity. The V region subgroups of the light chains were determined by both sequence and antigenic analysis. The latter procedure permitted large scale screening for comparisons with control proteins. The two methods showed general agreement in the determination of Kappa III proteins; all proteins positive by antigenic analysis were also positive by sequence but exceptions were noted in the opposite direction. The anti-γ-globulins showed by antigenic analysis a 92% incidence of VK III light chains as compared to an incidence of 27% among 81 control proteins without this activity. A similar selection was observed for an antigen (VK III b) which subdivided the kappa III proteins.