A mild method for the preparation of disulfide-linked hybrids of immunoglobulin light chains.
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 kappa chain (Jen) crystallizes in the same space group as an aggregate of monomers, but the unit cell is only one-third as large.
D001536:Bence Jones Protein; D055598:Chemical Phenomena; D002621:Chemistry; D003460:Crystallization; D004220:Disulfides; D004588:Electrophoresis, Cellulose Acetate; D004591:Electrophoresis, Polyacrylamide Gel; D007147:Immunoglobulin Light Chains; D011725:Pyridines; D013438:Sulfhydryl Compounds
D004220:Disulfides; D007147:Immunoglobulin Light Chains; D011725:Pyridines; D013438:Sulfhydryl Compounds; D001536:Bence Jones Protein