Abstract
The hemolytic activity of 5-n-alk(en)ylresorcinols [from Secale coreale] is temperature dependent and correlated to their transition temperatures. The values of the parameters describing the 5-n-alk(en)ylresorcinol-induced red blood cell lysis indicate strong affinity of the compounds to the membrane and their high lytic capacity. The affinity of the compounds for the membrane decrease with the increasing quantity of the molecules incorporated into the erythrocyte membrane and is much higher for saturated resorcinols than unsaturated ones. The amount of 5-n-alk(en)ylresorcinol molecules bound to the membrane at a 100% lysis is .apprx. 80 and 11 times (for alkyl and alkenyl derivatives, respectively), higher than at 0% lysis. Estimated free energy of erythrocyte lysis was similar for alkyl and alkenyl derivatives of resorcinol provided the preparation of the resorcinolic suspensions above their transition temperatures.