The organophosphorus insecticide bromfenvinfos (2-bromo-l-(2,4-dichlorophenyl)vinyl diethyl phosphate) and its methylated homologue methylbromfenvinfos inhibited noncompetitively the activity of (Ca2+ + Mg2+)-ATPase bound to and solubilized from pig erythrocyte membrane. Both enzyme preparations exhibited biphasic substrate curves displaying the existence of two functional active sites with low and high affinity to ATP. Inhibition of activity was more pronounced for bromfenvinfos than for methylbromfenvinfos and the solubilized enzyme preparation was more affected than the bound one. The results of the experiment suggest that the insecticides inhibited the ATPase by binding to a site on the enzyme rather than by interaction with associated lipids, although their presence could weaken the action of the compounds due to the stronger affinity of organophosphorus insecticides for lipids rather than for proteins.
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