A mild method for the preparation of disulfide-linked hybrids of immunoglobulin light chains
| Autor: | Allen B. Edmundson, Xiao-Min He, D. L. Montgomery, J. A. Oster, Kathryn R. Ely, Debra L. Harris, D. C. Shaw |
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| Rok vydání: | 1987 |
| Předmět: |
chemistry.chemical_classification
Chemical Phenomena Pyridines Dimer Immunology Electrophoresis Cellulose Acetate Immunoglobulin light chain Dithiothreitol chemistry.chemical_compound Chemistry Monomer Biochemistry chemistry Covalent bond Polymer chemistry Thiol Molecule Electrophoresis Polyacrylamide Gel Immunoglobulin Light Chains Disulfides Sulfhydryl Compounds Crystallization Molecular Biology Polyacrylamide gel electrophoresis Bence Jones Protein |
| Zdroj: | Molecular immunology. 24(3) |
| ISSN: | 0161-5890 |
| Popis: | A method is described for the hybridization of immunoglobulin light chains (Bence-Jones proteins) from different patients. The interchain half-cystine residues in the light chains from one subject are converted into mixed disulfides with 2,2'-dithiodipyridine. In the Bence-Jones dimer from a second patient the interchain disulfide bond is reduced with dithiothreitol. A covalently linked hybrid molecule is produced by the reaction of the mixed disulfide with the reduced thiol. In favorable cases the mild treatment yields heterodimers which can be crystallized for X-ray diffraction studies. The procedure can also be employed for converting a monomer into a covalent dimer. The engineered dimer of one κ chain (Jen) crystallizes in the same space group as an aggregate of monomers, but the unit cell is only one-third as large. |
| Databáze: | OpenAIRE |
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