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The oxidative degradation of urate to allantoin and CO2 is catalyzed by the enzyme uricase. Its activity was determined in the presence of two potassium cyanatum preparations in the dilution step D8, which differed by the method of preparation. While variant 1 (homoeopathic D8) was prepared homoeopathically, variant 2 (electronic D8) was produced electronically.The target of these studies was to investigate the impact of homoeopathic and electronic D8 on the catalytic activity of uricase.In the presence of these tow D8 variants, the enzymic degradation of urate was determined by a spectrophotometric assay over a period of 10 minutes.1. In the presence of homoeopathic D8 a stimulation of enzyme activity was detected. 2. In the case of electronic D8 neither a stimulation nor an inhibition of enzyme-catalyzed urate degradation was observed. 3. The differences in the effect of homoeopathic and electronic D8 on uricase were found to be statistically relevant.With the help of a cell-free system, such as uricase, it is possible to detect differing effects of homoeopathically and electronically prepared D8. In contrast to the electronic D8, the homoeopathic D8 is capable of modulating the enzyme activity. This observation leads to the assumption that homoeopathically prepared drugs are superior in their therapeutical efficiency to electronically produced drugs. However, the interpretation would be allowed, too, that the cell-free system used in this study, which has been isolated from an organism, is no longer in a position to react to an electronically prepared potency.