S-sulfonation: a reversible chemical modification of human immunoglobulins permitting intravenous application. I. Physicochemical and binding properties of S-sulfonated and reconstituted IgG.
S-sulfonation represents a reversible chemical modification of disulfide bonds by which under the special conditions chosen only about 2.2 cystine units per IgG molecule are cleaved. Physicochemical and functional evidence for reconstitution is presented. Molecules reconstituted in vitro or in vivo regain, within a few hours, a reactivity (antigen binding, immunoprecipitation, Clq-mediated cross-linking of immune complexes) comparable to equimolar control preparations.
D000818:Animals; D000888:Antibodies, Anti-Idiotypic / Q000096:biosynthesis; D000936:Antigen-Antibody Complex / Q000378:metabolism; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D003166:Complement Activating Enzymes / Q000378:metabolism; D015922:Complement C1q; D003165:Complement System Proteins / Q000276:immunology; D006207:Half-Life; D006801:Humans; D007070:Immunoglobulin A / Q000032:analysis; D007074:Immunoglobulin G / Q000008:administration & dosage* / Q000145:classification / Q000378:metabolism; D007075:Immunoglobulin M / Q000032:analysis; D008623:Mercaptoethanol / Q000494:pharmacology; D011817:Rabbits
D000888:Antibodies, Anti-Idiotypic; D000936:Antigen-Antibody Complex; C021306:IgG, sulfonated; D007070:Immunoglobulin A; D007074:Immunoglobulin G; D007075:Immunoglobulin M; D008623:Mercaptoethanol; D015922:Complement C1q; D003165:Complement System Proteins; D003166:Complement Activating Enzymes