Reconstitution of the liver microsomal monooxygenase system in liposomes from dimyristoylphosphatidylcholine
Kisselev, P.A.; Smettan, G.; Kissel, M.A.; Elbe, B.; Zirwer, D.; Gast, K.; Ruckpaul, K.; Akhrem, A.A.
Biomedica Biochimica Acta 43(3): 281-293
1984
ISSN/ISBN: 0232-766X PMID: 6743304 Document Number: 224188
Different techniques to incorporate the essential isolated and purified enzymes of rabbit hepatic endoplasmic reticulun 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 microscopy and EM the structural properties of the reconstituted system were proved comparing the reduction of cytochrome 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 cytochrome P-450 LM2 in soluble and liposomal form.