Abstract

The human T cell antigen-receptor gamma chain, which is expressed on the surface of a subpopulation of CD3+ T lymphocytes, exhibits size polymorphism and varies in its ability to form disulfide bonds with a second polypeptide. Analysis of both genomic and complementary DNA clones encoding the human gamma polypeptide shows differences in lengths of the coding portions of the two constant region genes, C gamma 1 and C gamma 2. A single second-exon segment is always present in the C gamma 1 gene. C gamma 2 alleles containing either duplicated or triplicated second-exon segments are present in the normal human population and are expressed as messenger RNAs. Furthermore, a cysteine residue, encoded by the second exon of C gamma 1 and probably involved in interchain disulfide bridging, is absent in all C gamma 2 second-exon segments. These differences between C gamma 1 and the two alleles of C gamma 2 may explain the variability in molecular weight and disulfide bonding of gamma molecules expressed in different cells.

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