[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.
D000818:Animals; D003577:Cytochrome P-450 Enzyme System / Q000378:metabolism*; D008297:Male; D008748:Methylcholanthrene / Q000494:pharmacology; D008862:Microsomes, Liver / Q000187:drug effects / Q000201:enzymology*; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D010634:Phenobarbital / Q000494:pharmacology; D051381:Rats
D008748:Methylcholanthrene; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; D010634:Phenobarbital
Samosborka membrannoĭ mikrosomnoĭ monooksigenaznoĭ sistemy pri gel'-fil'tratsii cherez sefadeks LH-20.