Separation and purification of multiple forms of microsomal cytochrome P-450. Partial characterization of three apparently homogeneous cytochromes P-450 prepared from livers of phenobarbital- and 3-methylcholanthrene-treated rats

This publication has 53 references indexed in Scilit:

• Amino-terminal sequence of phenobarbital-inducible cytochrome P-450 from rabbit liver microsomes: Similarity to hydrophobic amino-terminal segments of preproteins
  Biochemical and Biophysical Research Communications, 1977
• A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
  Analytical Biochemistry, 1976
• Purification of a substrate complex of cytochrome P-450 from liver microsomes of 3-methylcholanthrene-treated rabbits
  Biochemical and Biophysical Research Communications, 1976
• Highly purified cytochrome P-448 and P-450 from rat liver microsomes
  Biochemical and Biophysical Research Communications, 1975
• A gel-electrophoretically homogeneous preparation of cytochrome P-450 from liver microsomes of phenobarbital-pretreated rabbits
  Biochemical and Biophysical Research Communications, 1974
• Multiplicity of cytochrome P450 hemoproteins in rat liver microsomes
  Biochemical and Biophysical Research Communications, 1974
• Comparison of the mixed function oxidase-catalyzed metabolism of a series of dialkyl p-nitrophenyl phosphorothionates
  Toxicology and Applied Pharmacology, 1972
• Four gel systems for electrophoretic fractionation of membrane proteins using ionic detergents
  Journal of Supramolecular Structure, 1972
• Chemical characterization of cytochrome P-450cam
  Biochemical and Biophysical Research Communications, 1970
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970