Proteoliposomes, containing cytochrome P450 1A2, were obtained by the chola
te-dialysis technique. The effect of bifunctional cross-linking reagents on
the purified hexameric cytochrome P450 1A2 in an aqueous medium and on the
proteoliposomal P450 1A2 have been compared. Electrophoretic analysis of t
he modified proteins demonstrated the same oligomeric (hexameric) organizat
ion of the hemoprotein in each case.