A marmoset T-lymphocyte protein related to defined human serum immunoglobulin and fragments.

Current concepts of the antigen-specific receptor of thymus-derived (T) lymphocytes suggest that this molecule bears immunoglobulin (Ig) variable (V) regions, but does not represent a classical serum antibody. We immunized rabbits with a globulin fraction obtained from an in vitro cultured marmoset T cell lymphoma line which expressed surface components related to immunoglobulins. Quantitative immunoprecipitation and competition radioimmunoassay studies carried out using characterized monoclonal human Igs and their chains and fragments show that this rabbit antiserum, raised against a T cell product, reacts with a particular, conformational VH-determinant which is formed by interaction with lambda light chains and with two mu chain (IgM) related determinants. Neither mu chain determinant is a major isotype specific marker, and each occurs only on certain distinct subsets of serum mu chains. One is located in the Fc fragment; the location of the other mu related determinant is not known. These results show that this rabbit antiserum recognizes both variable and constant region determinants on the T cell receptor heavy chain. Rabbit antibody to the T cell product which cross-reacts with serum mu chain was isolated by immune affinity chromatography on Sepharose-derivatized covalently with one particular reactive IgM protein, the Waldenstrom macroglobulin Can (kappa mu). This antibody precipitated a biosynthetically-labelled component of approximate M.W. 70,000 as assessed by polyacrylamide gel electrophoresis in Na Dod SO4-containing buffers. These data support the conclusion that certain T cells express and synthesize a molecule related to Ig VH-regions which also has a constant region sharing antigenic markers with IgM subpopulations.