| http://purl.uniprot.org/citations/10833273 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10833273 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10833273 | http://www.w3.org/2000/01/rdf-schema#comment | "We previously reported the cloning of a human liver leukotriene B(4) (LTB(4)) omega-hydroxylase P450 designated CYP 4F2 [Kikuta et al. (1994) FEBS Lett. 348, 70-74]. However, the properties of CYP 4F2 remain poorly defined. The preparation solubilized using n-octyl-beta-D-glucopyranoside from microsomes of CYP 4F2-expressing yeast cells catalyzes v-hydroxylation of LTB(4), 6-trans-LTB(4), lipoxin A(4), 8-hydroxyeicosatetraenoate, 12-hydroxyeicosatetraenoate, and 12-hydroxystearate in the presence of rabbit liver NADPH-P450 reductase. In addition, the enzyme shows ethoxycoumarin O-deethylase and p-nitroanisole O-demethylase activities. The enzyme was purified to apparent electrophoretic homogeneity from yeast cells by sequential chromatography of solubilized microsomes through amino-n-hexyl-Sepharose 4B, DEAE-HPLC, and hydroxylapatite HPLC columns. The final preparation showed a specific content of 11.1 nmol of P450/mg of protein, with an apparent molecular mass of 56.3 kDa. CYP 4F2 was distinguished from the closely homologous CYP 4F3 (human neutrophil LTB(4) omega-hydroxylase) by its much higher K(m) for LTB(4), inability to omega-hydroxylate lipoxin B(4), and extreme instability."xsd:string |
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| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/author | "Kikuta Y."xsd:string |
| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/author | "Kikuta Y."xsd:string |
| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/author | "Kusunose E."xsd:string |
| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/author | "Kusunose E."xsd:string |
| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/author | "Kusunose M."xsd:string |
| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/author | "Kusunose M."xsd:string |
| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/pages | "1047-1052"xsd:string |
| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/pages | "1047-1052"xsd:string |
| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/title | "Characterization of human liver leukotriene B(4) omega-hydroxylase P450 (CYP4F2)."xsd:string |
| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/title | "Characterization of human liver leukotriene B(4) omega-hydroxylase P450 (CYP4F2)."xsd:string |
| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/volume | "127"xsd:string |
| http://purl.uniprot.org/citations/10833273 | http://purl.uniprot.org/core/volume | "127"xsd:string |
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| http://purl.uniprot.org/citations/10833273 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10833273 |
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| http://purl.uniprot.org/citations/10833273 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10833273 |