Abstract
Abstract Human synovial fluid, obtained post mortem from knee joints, has been found to hydrolyse p -nitrophenyl-N-acetyl-β- d -glucosaminide to p -nitrophenol and N-acetyl glucosamine. The activity was measured at 37° and pH 4.5. Sodium aurothiomalate (“Myocrisin”) non-competitively inhibits this glucosaminidase activity. Gold tribromide and p -chloromercuribenzoate also inhibit the glucosaminidase activity. Inhibition by “Myocrisin” was observed at concentrations within the range that might be reached in the treatment of rheumatoid arthritis.
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