Abstract
Introduction
In our laboratory we have focused on several enzymes, among them β-glucuronidase, which have been shown to be released in abnormal quantities during chronic inflammatory diseases such as Rheumatoid Arthritis.1,2 This enzyme, which is involved in the catalysis of β-glucuronides, has been characterized in mammalian tissues.3 In previous studies4,5 we have demonstrated that it was inhibitied by a number of synthetic antiinflammatory gold (I) complexes, such as gold (I) thiomalate (Myochrisin) and gold (I) thiosulfate (Solganol). although the mechanism of inhibition has not been verified we have suggested from these and previous studies6 that a thiol group on the enzyme may be the primary site of binding to the gold complex.