Literature DB >> 2089036

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

S Ishihara1, K Morohashi, H Sadano, S Kawabata, O Gotoh, T Omura.   

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.

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Year:  1990        PMID: 2089036     DOI: 10.1093/oxfordjournals.jbchem.a123310

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  3 in total

1.  Identification of a novel protein MICS1 that is involved in maintenance of mitochondrial morphology and apoptotic release of cytochrome c.

Authors:  Toshihiko Oka; Tomoko Sayano; Shoko Tamai; Sadaki Yokota; Hiroki Kato; Gen Fujii; Katsuyoshi Mihara
Journal:  Mol Biol Cell       Date:  2008-04-16       Impact factor: 4.138

2.  Human cystathionine beta-synthase: gene organization and expression of different 5' alternative splicing.

Authors:  J F Chassé; V Paul; R Escañez; P Kamoun; J London
Journal:  Mamm Genome       Date:  1997-12       Impact factor: 2.957

3.  Comparison of the 5' end of the rat and mouse cystathionine beta-synthase genes.

Authors:  M D Roper; J R Straubhaar; E Kraus; J Sokolová; M Hrebícek; J P Kraus
Journal:  Mamm Genome       Date:  1996-10       Impact factor: 2.957

  3 in total

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