MOLECULAR PROPERTIES OF T LYMPHOMA IMMUNOGLOBULIN

Abstract

Immunoglobulin (Ig) released into the medium by monoclonal continuously cultured murine T lymphoma cells of the lines WEHI-22 and WEHI-7 was isolated by serological precipitation or solid-phase immunoadsorption techniques. The intact immunoglobulin had an electrophoretic mobility on sodium dodecyl-sulphate (SDS) containing polyacrylamide gels comparable to that of IgG (mass 150,000). This mobility was significantly faster than that of ‘7S’ IgM of murine B lymphocyte surfaces. The T lymphoma immunoglobulin consisted of a pair of heavy chains linked by disulphide bonds and light chains non-covalently bound to the heavy chains. The isolated heavy chains migrated slightly faster than the μ chains of MOPC 104E IgM. Some, but not all, antisera directed against μ chains of normal mouse serum IgM bound T lymphoma immunoglobulin apparently via a cross-reaction localized to the F_d fragment. These data indicate that immunoglobulin of T lymphoma cells and, presumably normal T lymphocytes, represents an immunoglobulin isotype which is distinct from those immunoglobulins found on the B cell surface.