The complete amino acid sequence of a constitutive form of liver microsomal cytochrome P-450.

This publication has 18 references indexed in Scilit:

• Use of a monoclonal antibody specific for rabbit microsomal cytochrome P-450 3b to characterize the participation of this cytochrome in the microsomal 6.beta.- and 16.alpha.-hydroxylation of progesterone
  Biochemistry, 1984
• The covalent structure of hepatic microsomal epoxide hydrolase. II. The complete amino acid sequence.
  Journal of Biological Chemistry, 1984
• Isolation and sequence analysis of three cloned cDNAs for rabbit liver proteins that are related to rabbit cytochrome P-450 (form 2), the major phenobarbital-inducible form
  Biochemistry, 1984
• Complete amino acid sequence and predicted membrane topology of phenobarbital-induced cytochrome P-450 (isozyme 2) from rabbit liver microsomes.
  Proceedings of the National Academy of Sciences, 1983
• Identification and localization of amino acid substitutions between two phenobarbital-inducible rat hepatic microsomal cytochromes P-450 by micro sequence analyses.
  Proceedings of the National Academy of Sciences, 1983
• Functional and structural polymorphism of rabbit microsomal cytochrome P-450 form 3b.
  Journal of Biological Chemistry, 1982
• Primary structure of a cytochrome P-450: coding nucleotide sequence of phenobarbital-inducible cytochrome P-450 cDNA from rat liver.
  Proceedings of the National Academy of Sciences, 1982
• Induction by Triacetyloleandomycin and partial purification of a LM3 form of cytochrome P-450 from rabbit liver microsomes
  Biochemical and Biophysical Research Communications, 1982
• Purification and properties of P-450lm3b, a constitutive form of cytochrome P-450, from rabbit liver microsomes
  Biochemical and Biophysical Research Communications, 1979
• [20] Reduction and S-carboxymethylation of proteins
  Published by Elsevier ,1967