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rdf:type |
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lifeskim:mentions |
umls-concept:C0001413,
umls-concept:C0021467,
umls-concept:C0021469,
umls-concept:C0027303,
umls-concept:C0030016,
umls-concept:C0048554,
umls-concept:C0851285,
umls-concept:C0851827,
umls-concept:C1549542,
umls-concept:C1701901,
umls-concept:C1882726
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pubmed:issue |
3
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pubmed:dateCreated |
1980-5-14
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pubmed:abstractText |
Perfusion of rat livers with 10 mM-fructose or pretreatment of the rat with 6-aminonicotinamide (70 mg/kg) 6 h before perfusion decreased intracellular ATP concentrations and increased the rate of p-nitroanisole O-demethylation. This increase was accompanied by a decrease in the free [NADP+]/[NADPH] ratio calculated from concentrations of substrates assumed to be in near-equilibrium with isocitrate dehydrogenase. After pretreatment with 6-aminonicotinamide the [NADP+]/[NADPH] ratio also declined. Reduction of NADP+ during mixed-function oxidation may be explained by inhibition of of one or more NADPH-generating enzymes. Glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, isocitrate dehydrogenase and "malic" enzyme, partially purified from livers of phenobarbital-treated rats, were inhibited by ATP and ADP. Inhibitor constants of ATP for the four dehydrogenases varied considerably, ranging from 9 micrometer for "malic" enzyme to 1.85 mM for glucose 6-phosphate dehydrogenase. NADPH-cytochrome c reductase was also inhibited by ATP (Ki 2.8 mM) and by ADP (Ki 0.9 mM), but not by AMP. Concentrations of ATP and ADP that inhibited glucose 6-phosphate dehydrogenase and the reductase were comparable with concentrations in the intact liver. Thus agents that lower intracellular ATP may accelerate rates of mixed-function oxidation by a concerted mechanism involving deinhibition of NADPH-cytochrome c reductase and one or more NADPH-generating enzymes.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-13110753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-14114860,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-209290,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-23104,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-4149252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-4154892,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-4206907,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-4244711,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-4390651,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-4391643,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-4404466,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-4774126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-5443994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-5500310,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-5673437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-5794230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-632295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-668699,
http://linkedlifedata.com/resource/pubmed/commentcorrection/44195-870683
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-nitroanisole,
http://linkedlifedata.com/resource/pubmed/chemical/6-Aminonicotinamide,
http://linkedlifedata.com/resource/pubmed/chemical/Adenine Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Anisoles,
http://linkedlifedata.com/resource/pubmed/chemical/Fructose,
http://linkedlifedata.com/resource/pubmed/chemical/NADH, NADPH Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/NADP,
http://linkedlifedata.com/resource/pubmed/chemical/NADPH Dehydrogenase,
http://linkedlifedata.com/resource/pubmed/chemical/NADPH-Ferrihemoprotein Reductase,
http://linkedlifedata.com/resource/pubmed/chemical/Nitroanisole O-Demethylase,
http://linkedlifedata.com/resource/pubmed/chemical/Nitrophenols
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
184
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
675-81
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pubmed:dateRevised |
2010-9-1
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pubmed:meshHeading |
pubmed-meshheading:44195-6-Aminonicotinamide,
pubmed-meshheading:44195-Adenine Nucleotides,
pubmed-meshheading:44195-Adenosine Triphosphate,
pubmed-meshheading:44195-Animals,
pubmed-meshheading:44195-Anisoles,
pubmed-meshheading:44195-Female,
pubmed-meshheading:44195-Fructose,
pubmed-meshheading:44195-Liver,
pubmed-meshheading:44195-NADH, NADPH Oxidoreductases,
pubmed-meshheading:44195-NADP,
pubmed-meshheading:44195-NADPH Dehydrogenase,
pubmed-meshheading:44195-NADPH-Ferrihemoprotein Reductase,
pubmed-meshheading:44195-Nitroanisole O-Demethylase,
pubmed-meshheading:44195-Nitrophenols,
pubmed-meshheading:44195-Oxidation-Reduction,
pubmed-meshheading:44195-Perfusion,
pubmed-meshheading:44195-Rats
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pubmed:year |
1979
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pubmed:articleTitle |
Regulation of p-nitroanisole O-demethylation in perfused rat liver. Adenine nucleotide inhibition of NADP+-dependent dehydrogenases and NADPH-cytochrome c reductase.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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