Inhibition of denaturation of human gamma globulin by a mixture of l‐histidine, l‐cystine, and copper, and its clinical implication in rheumatoid arthritis

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Abstract
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.
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