Lymphocyte specific heterogeneity in the rat leucocyte common antigen (T200) is due to differences in polypeptide sequences near the NH2-terminus.

The leucocyte-common antigen (L-CA, T200 or CD45) consists of a family of heavily glycosylated glycoproteins of apparent Mr 180,000-240,000 which are restricted to lymphoid and myeloid cells. Forms of L-CA which differ in their apparent Mr, antigenicity and glycosylation are expressed on different lymphocyte types. One specific antigenic determinant called MRC OX-22 is of particular interest because it distinguishes two sets of T helper cells that have different functions. From the sequence of different L-CA cDNA clones we now conclude that there is sequence heterogeneity such that at least four forms of L-CA exist with sequences in the range 1118-1250 amino acids. All the sequence variation occurs at a point starting 6 residues from the NH2-terminus and the last 1112 residues of all forms are identical. Two of the variants can be directly related to the antigenic variation because they include sequence that was determined for a peptide that carries the MRC OX-22 determinant. Analysis of glycopeptides from thymocyte L-CA identified only one non-glycosylated position out of 14 possible N-glycosylation sites and established that all O-glycosylation was within the first 32 amino acids. The extra protein sequence in the longer forms was also suggestive of extensive O-glycosylation.