Molecular cloning and sequence analysis of cDNA coding for rat liver hemoprotein H-450

J Biochem. 1990 Dec;108(6):899-902. doi: 10.1093/oxfordjournals.jbchem.a123310.

Abstract

cDNA clones coding for hemoprotein H-450 were isolated from a rat liver cDNA library using anti-H-450 antibody. The molecular weight calculated from the deduced amino acid sequence comprising 547 amino acid residues was 60,085. The N-terminal sequence and a partial internal amino acid sequence of purified H-450, which were determined chemically, were both found in the amino acid sequence of H-450 deduced from the nucleotide sequence. H-450 mRNA is expressed in liver, kidney, and brain. A homology search of amino acid sequences indicated that H-450 shows no homology with cytochrome P-450, but shows significant homology with bacterial O-acetylserine (thiol)-lyases. However, H-450 has no O-acetylserine (thiol)-lyase activity.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibodies / immunology
  • Base Sequence
  • Cloning, Molecular
  • DNA / analysis*
  • Genomic Library
  • Hemeproteins / biosynthesis
  • Hemeproteins / genetics*
  • Liver / chemistry*
  • Molecular Sequence Data
  • Organ Specificity
  • RNA, Messenger / metabolism
  • Rats
  • Restriction Mapping
  • Sequence Homology, Nucleic Acid

Substances

  • Antibodies
  • Hemeproteins
  • RNA, Messenger
  • hemoprotein H-450
  • DNA