[Immunochemical analysis of two peak M proteinemia derived from structural differences of IgG Fc region].

We found M-proteins with two peaks by agarose electrophoresis in the serum of a myeloma patient. The M-proteins were identified as both IgG 1-kappa type, and classified as IgG-F (fast mobility) and IgG-S (slow mobility). 1) The possibility that the two M-proteins were derived from the post translational differences of sugar moieties of the same IgG molecule was unlikely, because no migration changes were observed in IgG-F and IgG-S after the treatment with 4 different sugar enzymes. 2) Fab fractions of IgG-F and IgG-S were analyzed. After papain or pepsin digestion, western blotting with anti-Fab antiserum revealed that the Fab fraction of IgG-F and IgG-S had identical mobility by agarose electrophoresis. However the Fc fractions of IgG-F and IgG-S analyzed by the same procedures with anti-Fe antiserum, were different. 3) Anti-idiotype antiserum prepared in rabbits against IgG-S, or -F, and absorbed by normal IgG and normal human serum showed a fused precipitin line with IgG-F and IgG-S. These findings suggest that two M-proteins with both IgG 1 and kappa type, have the same VH and VL regions but have different constant regions of heavy chain. Since one copy of IgG 1 constant gene is found in each human haploid gene. It is speculated that the switching of the rearranged VDJ gene to constant region gene occurred not only between cis chromosome but also between trans chromosome.