Characterization of differing effects caused by homeopathically prepared and conventional dilutions using cytochrome P450 2E1 and other enzymes as detection systems.

Determination of cytochrome P450 2E1 activity was carried out via hydroxylation of the synthetic substrate p-nitrophenol to p-nitrocatechol. Crude microsomal preparation isolated from rat liver served as source for cytochrome P450 2E1. Under assay conditions guaranteeing a linear course of the reaction the cytochrome P450 2E1 was stimulated in the presence of a 10(-6) dilution of As2O3 corresponding to 0.915 microM final concentration compared with control. All other concentrations of As2O3 used inhibited the enzyme activity more or less drastically. Furthermore, we used this enzyme system to study the influence of arsenicum album (As2O3) and potassium cyanatum (KCN) in homeopathically prepared (i.e., by consecutive 1:10 steps) and conventional dilutions. We found significant differences between the effects caused by homeopathic potencies (D) and equally concentrated dilutions on catalytic activity of cytochrome P450 2E1. Such differing effects were observed in the case of arsenicum album (As2O3) between D4/10(-4) and D6/10(-6) and in the case of potassium cyanatum (KCN) between D6/10(-6) and D12/10(-12). When we used glutathione-S-transferases and uricase we also found different effects mediated by potencies and conventional dilutions. The results obtained suggest that these three enzyme systems are appropriate detection systems to hunt out differing effects of differently prepared dilutions of specific test substances.