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- Title
The Extracellular Portion of HLA-DR α Chain is Composed of Two Compactly Folded Domains.
- Authors
Bill, P.; Lind, P.; Rask, L.; Peterson, P. A.
- Abstract
A truncated form of the class II antigen DRα chain of the human major histoeompatibility complex was produced in bacteria. A cDNA clone encoding the intact chain was modified so that the segment encoding the signal sequence was replaced by an ATG codon and the 3′ region downstream to the part corresponding to the third exon was replaced by a stop codon. The new construct was put under the control of the Tae promoter in a bacterial expression vector. The distance between the Shine-Delgarno sequence and the initiation codon was randomized so that clones with optimal expression of the truncated DRα chain could be obtained after induced expression and immunoscreening. The truncated DR a chain was subjected to limited proteolysis with chymotrypsin, and the resulting cleavage products were analysed by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Two fragments were visualized by western blotting. Electrophoresis in the absence and presence of reducing agents suggested that one of the proteolytic fragments contained a disulphide bridge. It is concluded that the extracellular portion of the DRα chain is composed of two compactly folded domains connected by an extended stretch of the polypeptide chain.
- Subjects
HLA class II antigens; PHASE partition; MOLECULAR cloning; GEL electrophoresis; HLA histocompatibility antigens; MOLECULAR genetics; ELECTROPHORESIS
- Publication
Scandinavian Journal of Immunology, 1987, Vol 26, Issue 3, p255
- ISSN
0300-9475
- Publication type
Article
- DOI
10.1111/j.1365-3083.1987.tb02259.x