Abstract
The effect of chlorhexidine (Chx) on some biochemical parameters of rat liver microsomes was studied. At concentrations of Chx above 100 μM a precipitate was formed with the microsomes and the precipitate was maximal above 200 μM. The major part of the microsomal proteins was also precipitated at concentrations of Chx exceeding 200 μM. When the concentration of Chx was higher than 75 μM cytochrome P‐450 was partly precipitated and partly converted to cytochrome P‐420. A concentration dependent inhibition of p‐nitro‐anisole‐O‐demethylase was observed, the activity being almost totally inhibited at 600 μM. The activity of microsomal glucose‐6‐phosphatase was markedly enhanced (70‐80 %) by Chx at concentrations above 75 μM although the activity of the enzyme was precipitated by Chx. The microsomes bound increasing amounts of Chx with increasing concentrations of the compound until about 1000 μM at which concentration the binding was maximal.
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