The Effect of Chlorhexidine on some Enzyme Activities of Rat Liver Lysosomes and Peroxisomes

Abstract

The effect of chlorhexidine (Chx) on some enzyme activities of rat liver lysosomes and peroxisomes was studied. A concentration dependent stimulation of lysosomal acid phosphatase was observed, the stimulation being maximal above 300 μM Chx. The acid phosphatase activity was released to an extent of 50% by Chx as compared to a release of nearly 100% caused by Triton X‐100. The lysosomal β‐N‐acetylglucosaminidase activity was stimulated by Chx with a maximum at 50 μM Chx. At higher concentrations of Chx the activity declined and above 300 μM the activity reached the level of the control. The activity was not significantly solubilized by Chx as compared to about 90% solubilized by 0.1% Triton X‐100. The peroxisomal catalase activity was precipitated almost totally at 3000 x g by 1000 μM Chx and the catalase activity was 50% depressed at 100 μM Chx and 70% at 1000 μM Chx. Peroxisomal urate oxidase was stimulated slightly by Chx. The activity reached a constant level of 125% of the control above 100 μM Chx. No activity was released from the peroxisomes by Chx. The mode of action of Chx is discussed in the light of the present results.

The Comparative Effect of Chlorhexidine and Cetrimonium Bromide on Erythrocyte Membranes

“…1975;JENSEN et d. 1975). It has been suggested that these effects of chlorhexidine on the lipoprotein membranes may be attributed to a non-specific cationic detergent effect (CHRISTENSEN et al 1975;JENSEN et al 1975). Since chlorhexidine influences the membranes and membrane-bound enzyme activities of microsomes, mitochondria, lysosomes and peroxisomes it was found to be of interest to examine the effects of chlorhexidine on the plasma-membrane of animal cells.…”