title: Covalent immunoglobulin assembly in vitro: reactivity of light chain covalent dimers (L2) and blocked light chain monomers.
abstract: Covalent light chain dimers (L2) and cysteine-blocked L chain monomers readily react with partially reduced heavy (H) chains. A rapid disappearance of these blocked L chain species is followed by the appearance of covalent intermediates-HL, H2, and H2L-leading to fully assembled H2L2. The mechanism of initial disulfide bond formation between heavy and light chains is disulfide interchange.
mesh_terms: D001536:Bence Jones Protein / Q000378:metabolism; D003545:Cysteine / Q000378:metabolism; D004220:Disulfides; D006801:Humans; D007074:Immunoglobulin G / Q000096:biosynthesis; D007143:Immunoglobulin Heavy Chains / Q000096:biosynthesis; D007147:Immunoglobulin Light Chains / Q000096:biosynthesis; D007142:Immunoglobulin gamma-Chains / Q000096:biosynthesis; D007145:Immunoglobulin kappa-Chains / Q000096:biosynthesis; D066298:In Vitro Techniques; D010084:Oxidation-Reduction; D011487:Protein Conformation
chemical_list: D004220:Disulfides; D007074:Immunoglobulin G; D007143:Immunoglobulin Heavy Chains; D007147:Immunoglobulin Light Chains; D007142:Immunoglobulin gamma-Chains; D007145:Immunoglobulin kappa-Chains; D001536:Bence Jones Protein; D003545:Cysteine