Abstract
Two drugs D-penicillamine and gold sodium thiomalate, used in the treatment of rheumatoid arthritis, removed copper(II) bound to bovine serum albumin as measured by a spectral change of the copper-albumin adduct. Utilizing the esterase activity of serum albumin and its inhibition by copper, it appears that the action of gold sodium thiomalate is indirect: serum albumin first reacted with the drug still bound copper, but addition of more drug did not remove it. Thus, the initial reaction of gold sodium thiomalate with albumin's free sulfhydryl group was required to make the thiomalate ligand available for reaction with copper bound at a different site.
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