Lyt-2 glycoprotein is synthesized as a single molecular species.

We investigated the possibility that the Lyt-2 molecules made by uncloned mouse T lymphocytes would show variable primary structures like those of immunoglobulins. Newly synthesized Lyt-2/3 complexes were found to include only two major components, both discrete glycoproteins with apparent molecular weights of 31,000 (31 K) and 35,000 (35 K). When products of Lyt-2.1 and Lyt-2.2 thymocytes were compared by two-dimensional nonequilibrium pH gradient electrophoresis and sodium dodecyl sulfate polyacrylamide gel electrophoresis, the isoelectric points of the 35 K molecules were different; thus, the 35 K component was likely to be encoded by the Lyt-2 locus itself. However, the 35 K molecules made by any one genotype were homogeneous in charge as well as in size. The homogeneity was obscured rapidly by post-translational modification. Most strikingly, within 30 min of initial synthesis, these processing events generated the conspicuous array of microheterogeneous products that form the "38 K" component of cell-surface Lyt-2/3.