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To obtain information about the structural basis for T-cell antigen recognition, a T3-associated Ti receptor molecule was isolated from crude membranes of the REX human thymic tumor line and purified by affinity chromatography with an anti- clonotypic monoclonal antibody in conjunction with preparative gel electrophoresis. NH2-terminal amino acid sequencing of the beta subunit unambiguously identified the amino acids in positions 2-12. Comparative protein sequence analysis by computer search demonstrated that this Ti beta sequence bore weak, but definite, homology to the first framework of the variable region of human lambda light chain. Anti-sera to a synthetic peptide corresponding to positions 2-11 precipitated the denatured Ti beta subunit from REX, thus confirming the above sequence. This information suggests that the Ti beta subunit is distantly related to human immunoglobulin lambda light chain and, moreover, should be of use in the molecular cloning of the Ti beta gene.

Type

Journal article

Journal

Proc Natl Acad Sci U S A

Publication Date

06/1984

Volume

81

Pages

3851 - 3855

Keywords

Amino Acid Sequence, Cells, Cultured, Humans, Immunoglobulin Light Chains, Macromolecular Substances, Molecular Weight, Receptors, Antigen, T-Cell, T-Lymphocytes