pubmed-article:2543147 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2543147 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
pubmed-article:2543147 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
pubmed-article:2543147 | lifeskim:mentions | umls-concept:C0205054 | lld:lifeskim |
pubmed-article:2543147 | lifeskim:mentions | umls-concept:C0025519 | lld:lifeskim |
pubmed-article:2543147 | lifeskim:mentions | umls-concept:C0023546 | lld:lifeskim |
pubmed-article:2543147 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:2543147 | lifeskim:mentions | umls-concept:C1979928 | lld:lifeskim |
pubmed-article:2543147 | lifeskim:mentions | umls-concept:C1705241 | lld:lifeskim |
pubmed-article:2543147 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:2543147 | lifeskim:mentions | umls-concept:C1705242 | lld:lifeskim |
pubmed-article:2543147 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:2543147 | pubmed:dateCreated | 1989-7-3 | lld:pubmed |
pubmed-article:2543147 | pubmed:abstractText | 1. The cytochrome P-450-dependent metabolism of leukotriene B4 (LTB4) by rat hepatic microsomes was characterized. Hepatic microsomes were found to metabolize LTB4 to 20-hydroxy-LTB4 and 20-carboxy:LTB4. The rate of formation of 20-hydroxy-LTB4 (14.6 pmol/min per mg protein) was 5.8-fold higher than that of 20-carboxy-LTB4 (2.5 pmol/min per mg protein). 2. LTB4 omega-hydroxylase activity required NADPH and oxygen indicating that the reaction is mediated by a mono-oxygenase system. The omega-hydroxylase activity was optimal at pH 7.4 and product formation was linear with respect to time of incubation and protein concentration. The reaction was significantly inhibited by carbon monoxide (89%), SKF 525-A (1 mM), and metyrapone (0.1 mM) whereas alpha-naphthoflavone had only marginal inhibitory effects. The apparent Km and Vmax of LTB4 omega-hydroxylase were 4 microM and 19.6 pmol/min per mg protein, respectively. 3. Ontogenic studies revealed that LTB4 omega-hydroxylase activity was low in 4-day-old rats and that there was a steady increase in enzyme activity as the animal matured. 4. Phenobarbital, 3-methylcholanthrene or Aroclor 1254 treatment of rats did not induce LTB4 omega-hydroxylase activity whereas clofibrate resulted in 61% induction in enzyme activity. No significant sex-dependent differences were observed. 5. It is concluded that hepatic metabolism of LTB4 may afford an effective mechanism for limiting many of the pro-inflammatory effects of circulating leukotrienes. | lld:pubmed |
pubmed-article:2543147 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2543147 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2543147 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2543147 | pubmed:language | eng | lld:pubmed |
pubmed-article:2543147 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2543147 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2543147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2543147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2543147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2543147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2543147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2543147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2543147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2543147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2543147 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2543147 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2543147 | pubmed:month | Feb | lld:pubmed |
pubmed-article:2543147 | pubmed:issn | 0049-8254 | lld:pubmed |
pubmed-article:2543147 | pubmed:author | pubmed-author:MukhtarHH | lld:pubmed |
pubmed-article:2543147 | pubmed:author | pubmed-author:DayGG | lld:pubmed |
pubmed-article:2543147 | pubmed:author | pubmed-author:BickersD RDR | lld:pubmed |
pubmed-article:2543147 | pubmed:author | pubmed-author:KhanW AWA | lld:pubmed |
pubmed-article:2543147 | pubmed:author | pubmed-author:BikD PDP | lld:pubmed |
pubmed-article:2543147 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2543147 | pubmed:volume | 19 | lld:pubmed |
pubmed-article:2543147 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2543147 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2543147 | pubmed:pagination | 151-9 | lld:pubmed |
pubmed-article:2543147 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:meshHeading | pubmed-meshheading:2543147-... | lld:pubmed |
pubmed-article:2543147 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2543147 | pubmed:articleTitle | Hepatic microsomal metabolism of leukotriene B4 in rats: biochemical characterization, effect of inducers, and age- and sex-dependent differences. | lld:pubmed |
pubmed-article:2543147 | pubmed:affiliation | Department of Dermatology, University Hospital of Cleveland, Case Western Reserve University, Ohio. | lld:pubmed |
pubmed-article:2543147 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2543147 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2543147 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:2543147 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:2543147 | lld:pubmed |