Inhibition of denaturation of human gamma globulin by a mixture of L-histidine, L-cystine, and copper, and its clinical implication in rheumatoid arthritis.
A mixture of histidine, cystine, and copper mimicked gold thiomalate, N-ethylmaleimide, and p-chloro-mercuribenzoic acid in inhibiting sulfhydryl-disulfide interchange-mediated denaturation of human gamma globulin, bovine serum albumin, and diluted human serum. Measurable inhibitory effects were obtained with a mixture of physiologic concentrations of L-histidine, L-cystine, and copper. This work suggests a mechanism by which the hypohistidinemia of rheumatoid arthritis could contribute to the pathogenesis of the disease.
D001172:Arthritis, Rheumatoid / Q000276:immunology*; D001798:Blood Proteins; D001809:Blood Viscosity / Q000187:drug effects; D002729:Chloromercuribenzoates / Q000494:pharmacology; D003300:Copper / Q000494:pharmacology*; D003553:Cystine / Q000494:pharmacology*; D004357:Drug Synergism; D005033:Ethylmaleimide / Q000494:pharmacology; D006052:Gold Sodium Thiomalate / Q000494:pharmacology; D006639:Histidine / Q000494:pharmacology*; D006358:Hot Temperature; D006801:Humans; D007460:Iodoacetamide / Q000494:pharmacology; D011489:Protein Denaturation / Q000187:drug effects*; D012710:Serum Albumin, Bovine; D005719:gamma-Globulins
D001798:Blood Proteins; D002729:Chloromercuribenzoates; D005719:gamma-Globulins; D006052:Gold Sodium Thiomalate; D012710:Serum Albumin, Bovine; D003553:Cystine; D006639:Histidine; D003300:Copper; D005033:Ethylmaleimide; D007460:Iodoacetamide