RT Journal Article
SR Electronic
T1 Preparation and Properties of a Solubilized Form of Cytochrome P-450 from Chick Embryo Liver Microsomes
JF Molecular Pharmacology
JO Mol Pharmacol
FD American Society for Pharmacology and Experimental Therapeutics
SP 280
OP 292
VO 7
IS 3
A1 F. MITANI
A1 A. P. ALVARES
A1 S. SASSA
A1 A. KAPPAS
YR 1971
UL http://molpharm.aspetjournals.org/content/7/3/280.abstract
AB A procedure for the partial purification and subsequent solubilization of cytochrome P-450 from microsomal membranes of chick embryo liver is described. Successive treatment of microsomes with Protease VII and Lubrol WX yielded a solubilized preparation with about a 1.8-fold increase in the specific content of cytochrome P-450, measured as millimicromoles per milligram of protein, with no detectable amounts of cytochrome b5 and minimal activities of NADPH- and NADH-cytochrome c reductases. The CO difference spectrum of the solubilized cytochrome P-450 showed an absence of cytochrome P-420; however, the absolute spectrum of the CO complex of the reduced preparation displayed a peak at 420 mµ. The solubilized cytochrome P-450 obtained from chick embryo livers interacted with various substrates to give type I or type II spectra similar to those observed in other species. Cytochrome P-450 in chick embryo liver was inducible by drugs, polycyclic hydrocarbons, and steroids.