[Reconstitution of membranous microsomal monooxygenase system during gel filtration on Sephadex LH-20].

Solubilization of liver microsomes of intact, phenobarbital-treated and 3-methylcholantrene-treated rats was investigated. It was shown that treatment of microsomes with 4% sodium cholate leads to separation of proteins and phospholipids from the microsomal membrane. The microsomal solubilizate was passed through lipophilic Sephadex LH-20 and the particles whose properties are close to those of the microsomal ones were obtained. The high efficiency of self-assembly of the microsome-like particles, e. g. lack of cytochrome P-450 conversion into cytochrome P-420, high microsomal protein yield and the high level of metabolizing activity of microsomal monooxygenase, was demonstrated.