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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.

Abstract:

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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Publication status:
Published

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Institution:
University of Oxford
Division:
MSD
Department:
Pathology Dunn School
Role:
Author
Journal:
Journal of biological chemistry More from this journal
Volume:
268
Issue:
3
Pages:
2013-2020
Publication date:
1993-01-01
EISSN:
1083-351X
ISSN:
0021-9258

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