| pubmed-article:7092814 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7092814 | lifeskim:mentions | umls-concept:C0205054 | lld:lifeskim |
| pubmed-article:7092814 | lifeskim:mentions | umls-concept:C0010762 | lld:lifeskim |
| pubmed-article:7092814 | lifeskim:mentions | umls-concept:C0680730 | lld:lifeskim |
| pubmed-article:7092814 | lifeskim:mentions | umls-concept:C0439857 | lld:lifeskim |
| pubmed-article:7092814 | lifeskim:mentions | umls-concept:C1979928 | lld:lifeskim |
| pubmed-article:7092814 | lifeskim:mentions | umls-concept:C2255333 | lld:lifeskim |
| pubmed-article:7092814 | lifeskim:mentions | umls-concept:C0549178 | lld:lifeskim |
| pubmed-article:7092814 | lifeskim:mentions | umls-concept:C1148554 | lld:lifeskim |
| pubmed-article:7092814 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:7092814 | pubmed:dateCreated | 1982-8-14 | lld:pubmed |
| pubmed-article:7092814 | pubmed:abstractText | 1. A continuous spectrophotometric determination of rat hepatic microsomal anaerobic azo reductase activity has been developed. 2. The addition of soluble flavins (riboflavin, FMN or FAD) greatly increased this NADPH-dependent activity towards a number of azo substrates. 3. Investigations with amaranth as substrate gave an apparent Km of 34 microM and Vmax. of 4 nmol/min per mg of microsomal protein. The inclusion of a fixed concentration of FMN increased Vmax. and greatly decreased Km, the magnitude of these changes reflecting the concentration of flavin present. 4. Investigations using a fixed amaranth concentration over a range of flavin concentrations gave biphasic double-reciprocal plots with two apparent Km and Vmax. values. 5. Pretreatment of animals with cobaltous chloride, 2-allyl-2-isopropylacetamide, carbon tetrachloride, phenobarbitone and 3-methylcholanthrene altered azo reductase activity in parallel with changes in cytochrome P-450 content. 6. The significance of these results is discussed in terms of the electron-transfer components present in the hepatic microsomal fraction. | lld:pubmed |
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| pubmed-article:7092814 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7092814 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7092814 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7092814 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7092814 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7092814 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:7092814 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:7092814 | pubmed:author | pubmed-author:WalkerRR | lld:pubmed |
| pubmed-article:7092814 | pubmed:author | pubmed-author:KingL JLJ | lld:pubmed |
| pubmed-article:7092814 | pubmed:author | pubmed-author:MallettA KAK | lld:pubmed |
| pubmed-article:7092814 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7092814 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7092814 | pubmed:volume | 201 | lld:pubmed |
| pubmed-article:7092814 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7092814 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7092814 | pubmed:pagination | 589-95 | lld:pubmed |
| pubmed-article:7092814 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7092814 | pubmed:year | 1982 | lld:pubmed |
| pubmed-article:7092814 | pubmed:articleTitle | A continuous spectrophotometric determination of hepatic microsomal azo reductase activity and its dependence on cytochrome P-450. | lld:pubmed |
| pubmed-article:7092814 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7092814 | pubmed:publicationType | In Vitro | lld:pubmed |
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