Separation, purification, and properties of multiple forms of cytochrome p-450 from the liver microsomes of phenobarbital-treated mice.

Abstract Four distinct cytochrome P-450 fractions (A1, A2, C1, and C2) have been separated and purified from the liver microsomes of phenobarbital-treated hybrid mice (B6D2F1/J). Fractions A2 and C2 were highly purified with specific contents of 16.5 and 17.5 nmol of cytochrome P-450/mg of protein, respectively, based on their amino acid compositions. The major hemeprotein bands of A2 and C2 have different minimum molecular weights (50,000 and 56,000, respectively) on polyacrylamide gels in the presence of sodium dodecyl sulfate. All four fractions with respect to their spectral and catalytic properties, thereby demonstrating that mouse liver microsomes from phenobarbital-treated hybrid mice contain at least four forms of cytochrome P-450.