[Isolation, analysis and characterization of microsomal ghost fractions].

A new method of isolating the microsomal ghost fractions has been developed. The membranes were purified from adsorbed protein, ribosomes and intravesicular content. The purified membranes contained 6 times less RNA than did the original microsomes. The phospholipid:protein ratio in the ghosts increased from 0.34 to 0.80. Protein electrophoretic pattern ghost was more homogenous than that of microsomes. SDS-polyacrylamide electrophoresis showed that the ghosts contain 11 fractions as compared to 21 in microsomes. A high degree of membrane purification did not affect the inactivation of microsomal enzymic systems. Practically all cytochrome P-450 in the ghosts was found in its active form. The activities of NAD(P)H-dependent systems of dimethylaniline and ethylmorphine demethylation, p-hydroxylation of aniline were well retained. The removal of non-membrane protein allows to obtain an electrone microscope picture of the lipid bilayer as a structural basis of microsomal membrane.