Activity of liver microsomal Ca2+-ATPase in relation to perturbation of membrane hydrophobic interactions induced by methoxybenzene derivatives and n-aliphatic alcohols.

Changes in the activity of liver microsomal Ca2+-ATPase were studied in the presence of two series of lipophilic compounds: four flavouring substances derived from methoxybenzene and four n-aliphatic alcohols. With each compound the activity was stimulated at lower concentrations and inhibited at higher concentrations. The linear relationship between equiactive concentrations of the compounds and their partition coefficients showed that the enzyme activity was modulated by perturbation of membrane hydrophobic interactions. Measurements carried out by electron-spin resonance (ESR) showed evidence of a decrease in the membrane order induced by these compounds. However, results obtained with the methoxybenzene derivatives showed that the modification in ATPase activity cannot be directly related to the decrease in membrane order. This decrease did not only reflect perturbation of hydrophobic interactions.