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.
| Original language | English |
|---|---|
| Pages (from-to) | 899-902 |
| Number of pages | 4 |
| Journal | Journal of Biochemistry |
| Volume | 108 |
| Issue number | 6 |
| DOIs | |
| Publication status | Published - 12-1990 |
| Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
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