Immunoglobulin degradation and D-penicillamine action.
Treatment of human IgG with pancreatic elastase gave a product of higher molecular weight than IgG. Its formation was inhibited by blocking IgG sulfhydryl groups with iodoacetamide. Incubation of the high molecular weight product with either glutathione or D-penicillamine yielded Fab- and Fc-like fragments. Addition of oxidized glutathione to mixtures containing either reduced thiol gave a new product of molecular weight intermediate between the high molecular weight product and Fab- and Fc-like fragments. Oxidized D-penicillamine did not substitute for oxidized glutathione. This new product was formed under conditions that favor protein sulfhydryl-disulfide exchange. The effect of D-penicillamine on its formation was discussed in terms of D-penicillamine's mode of action in rheumatoid arthritis.
D055598:Chemical Phenomena; D002621:Chemistry; D004220:Disulfides / Q000378:metabolism; D005978:Glutathione / Q000378:metabolism; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism*; D008970:Molecular Weight; D010084:Oxidation-Reduction; D010179:Pancreas / Q000201:enzymology; D010196:Pancreatic Elastase / Q000378:metabolism*; D010396:Penicillamine / Q000494:pharmacology*; D013438:Sulfhydryl Compounds / Q000378:metabolism
D004220:Disulfides; D007074:Immunoglobulin G; D013438:Sulfhydryl Compounds; D010196:Pancreatic Elastase; D005978:Glutathione; D010396:Penicillamine