Molecular properties of T-lymphoma immunoglobulin. III. Peptide composition of the light chain.
Structural studies of T-cell immunoglobulin light chains have been carried out in order to ascertain whether they possess a unique structure or if they resemble standard kappa or lambda isotypes. T-cell immunoglobulin was isolated from 125I-labelled culture medium of monoclonal, continuously cultured T-lymphoma cells, and the purified 125I-labelled light chains were subjected to either cleavage by cyanogen bromide or digestion with trypsin. These peptides were then resolved and compared with those derived from 125I- and 131I-labelled murine kappa and lambda chains in mixed label experiments, by means of polyacrylamide gel electrophoresis in sodium dodecyl sulfate-containing buffers and ion exchange chromatography. The profiles obtained suggested that T-lymphoma immunoglobulin light chains are immunoglobulin polypeptides and most closely resemble kappa chains. These results support available antigenic and mRNA hybridization data, which also suggest that T cells bear kappa-like light chains.
D000818:Animals; D002460:Cell Line; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007147:Immunoglobulin Light Chains / Q000032:analysis*; D007145:Immunoglobulin kappa-Chains / Q000032:analysis; D008223:Lymphoma; D051379:Mice; D010446:Peptide Fragments / Q000032:analysis*; D013601:T-Lymphocytes / Q000276:immunology*
D007147:Immunoglobulin Light Chains; D007145:Immunoglobulin kappa-Chains; D010446:Peptide Fragments