TY - JOUR
T1 - Molecular cloning and sequence analysis of cDNA coding for rat liver hemoprotein H-450
AU - Ishihara, Satoru
AU - Morohashi, Ken ichirou
AU - Sadano, Hiroyuki
AU - Kawabata, Shun ichiro
AU - Gotoh, Osamu
AU - Omura, Tsuneo
PY - 1990/12
Y1 - 1990/12
N2 - 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.
AB - 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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U2 - 10.1093/oxfordjournals.jbchem.a123310
DO - 10.1093/oxfordjournals.jbchem.a123310
M3 - Article
C2 - 2089036
AN - SCOPUS:0025696047
SN - 0021-924X
VL - 108
SP - 899
EP - 902
JO - Journal of Biochemistry
JF - Journal of Biochemistry
IS - 6
ER -