Intermolelular communication between a receptor incorporated into liposome and lactate dehydrogenase(LDH) adsorbed on the membrane was established on artificial membranes,mediated by Cu2+.The receptor,having a moiety of pseudo-crown ether binding K+ and two histidine residues binding Cu2+,is a gemini compound with heteroditopic ion recognition site of Cu2+ as an inhibitor of the enzyme and K+ as a stimulating signal.The relative activity of the enzyme was 40.9% due to the inhibition of Cu2+ in the absence of K +,up to 85.9% in the presence of K +.In the communication system,the K+ signal was transduced to LDH by the receptor,leading to enhancement of LDH activity.
