Heterogeneity in the membrane proteins of human lymphoid cell lines as seen in sodium dodecyl sulfate-polyacrylamide electrophoresis slab gels.

The proteins of [35S]methionine-labeled membranes of six human lymphoid cell lines were examined by electrophoresis in sodium dodecyl sulfate-polyacrylamide gradient slab gels in order to identify molecular differences among these tumors. The lymphoid cells were internally labeled with [35S]methionine, their membranes were isolated, and the reduced and alkylated membrane proteins were treated electrophoretically in sodium dodecyl sulfate-polyacrylamide gradient slab gels. The gel patterns of over 100 membrane proteins per cell were highly complex but reproducible and, in that sense, constituted fingerprints of the individual tumors. Several proteins occurred uniquely on one or a few tumors. Some protein bands were identified to be serologically recognized membrane antigens by electrophoresis of immunopurified antigen in parallel to membrane samples. p44,12, a complex of proteins with molecular weights of 44,000 and 12,000 (HLA-A and -B antigens and beta2-microglobulin), and p29,34, (HLA-D antigen) were identified in this manner. High-resolution sodium dodecyl sulfate-polyacrylamide gradient gel electrophoresis can be used to catalog and describe lymphocyte membrane proteins and perhaps to identify subsets of lymphoid cancers.