1976
DOI: 10.1002/art.1780190311
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Inhibition of denaturation of human gamma globulin by a mixture of l‐histidine, l‐cystine, and copper, and its clinical implication in rheumatoid arthritis

Abstract: A mixture of histidine, cystine, and copper mimicked gold thiomalate, N-ethylmaleimide, and pchloromercuribenzoic acid in inhibiting sulfbydryl-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 Lhistidine, Lcystine, and copper. This work suggests a mechanism by which the hypohistidinemia of rheumatoid arthritis could contribute to the pathogenesis of the … Show more

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Cited by 21 publications
(1 citation statement)
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“…Gold(I)-thiolate complexes and D-penicillamine have been hypothesised to reduce total biofluid copper levels via their interaction with Cu(II) ions bound to the N-terminal binding site located on albumin [15]. A mixture of histidine, cysteine and Cu(II) ions has been demonstrated to mimic disodium aurothiomalate in inhibiting the sulphydryl-disulfide interchange reaction-mediated denaturation of human gamma globulin, bovine serum albumin and diluted human serum [17].…”
Section: Introductionmentioning
confidence: 99%
“…Gold(I)-thiolate complexes and D-penicillamine have been hypothesised to reduce total biofluid copper levels via their interaction with Cu(II) ions bound to the N-terminal binding site located on albumin [15]. A mixture of histidine, cysteine and Cu(II) ions has been demonstrated to mimic disodium aurothiomalate in inhibiting the sulphydryl-disulfide interchange reaction-mediated denaturation of human gamma globulin, bovine serum albumin and diluted human serum [17].…”
Section: Introductionmentioning
confidence: 99%