Reconstitution of the liver microsomal monooxygenase system in liposomes from dimyristoylphosphatidylcholine.

Different techniques to incorporate the essential isolated and purified enzymes of the hepatic endoplasmic reticulum into monolamellar dimyristoylphosphatidylcholine vesicles are compared with respect to structural and functional parameters of the reconstituted system. By use of gel penetrating chromatography on Sepharose 4B, dynamic light scattering and electron microscopy the structural properties of the reconstituted system were proved comparing the reduction of P-450 LM2 via the NADPH dependent reductase and by dithionite as well with the microsomal reduction rates and by studying the binding of benzphetamine to P-450 LM2 in soluble and liposomal form.