Variants of a mouse myeloma cell line that synthesize immunoglobulin heavy chains having an altered serotype

Abstract

Cells of the MPC-11 mouse myeloma cell line, which produces an IgG2b immunoglobulin, were subjected to mutagenesis with Melphalan or with ICR-191, after which they were cloned in soft agar. Approximately 0.5 percent of the clones produced altered heavy chains that: (i) were the same size as or larger than the parent; (ii) no longer recognized by antibody specific for the parent gamma2b subclass; (iv) were recognized by antibody against the Fab (NH2-terminal half) of the parental immunoglobulin, but lacked some of the antigenic determinants of the Fc (COOH-terminal half) of the heavy chain; (v) lacked many of the tryptic/chymotryptic peptides found in the parent; (vi) contained tryptic/chymotryptic peptides that were not present in the parent but were present in an unrelated gamma2a myeloma heavy chain; and (vii) assembled with light chains by a pathway typical of IgG2a myelomas.