Evidence for an extended structure of the T-cell co-receptor CD8 alpha as deduced from the hydrodynamic properties of soluble forms of the extracellular region.

Journal article

We expressed soluble forms of the human T-cell coreceptor CD8 alpha extracellular region, CD8 alpha 161, and the amino-terminal immunoglobulin-like domain, CD8 alpha 114, in Chinese hamster ovary cells and Escherichia coli, respectively. Both molecules were readily purified to homogeneity in milligram amounts and were recognized by a large panel of monoclonal antibodies. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis indicated that approximately 70% of CD8 alpha 161 was se...

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Authors: Boursier, J; Alcover, A; Herve, F; Laisney, I; Acuto, O

• Publication status: Published
• Journal: Journal of biological chemistry
• Volume: 268
• Issue: 3
• Pages: 2013-2020
• Publication date: 1993-01-01
• EISSN: 1083-351X
• ISSN: 0021-9258
• Language: English
• Keywords: Mutagenesis, Site-Directed; Gene Expression; Antibodies, Monoclonal; Antigens, CD8; Electrophoresis, Polyacrylamide Gel; T-Lymphocytes; Chemistry, Physical; Humans; Base Sequence; Amino Acid Sequence; Solubility; Molecular Sequence Data; Physicochemical Phenomena; Cricetinae; Transfection; Escherichia coli; Animals; CHO Cells; Cloning, Molecular; Recombinant Proteins; DNA