| pubmed-article:1998730 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1998730 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:1998730 | lifeskim:mentions | umls-concept:C0162362 | lld:lifeskim |
| pubmed-article:1998730 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:1998730 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:1998730 | lifeskim:mentions | umls-concept:C1158368 | lld:lifeskim |
| pubmed-article:1998730 | lifeskim:mentions | umls-concept:C0308269 | lld:lifeskim |
| pubmed-article:1998730 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1998730 | pubmed:dateCreated | 1991-4-10 | lld:pubmed |
| pubmed-article:1998730 | pubmed:abstractText | Respiration-linked oxidation of 3-hydroxybutyryl-CoA, crotonyl-CoA and saturated fatty acyl (C4, C8 and C14)-CoA esters was studied in different mitochondrial preparations. Oxidation of acyl-CoA esters was poor in intact mitochondria; however, it was significant, as well as, NAD+ and CoA-dependent in gently and in vigorously sonicated mitochondria. The respiration-linked oxidation of crotonyl-CoA and 3-hydroxybutyryl-CoA proceeded at much higher rates (over 700%) in gently disrupted mitochondria than in completely disrupted mitochondria. The redox dye-linked oxidation of crotonyl-CoA (with inhibited respiratory chain) was also higher in gently disrupted mitochondria (149%) than in disrupted ones. During the respiration-linked oxidation of 3-hydroxybutyryl-CoA the steady-state NADH concentrations in the reaction chamber were determined, and found to be 8 microM in gently sonicated and 15 microM in completely sonicated mitochondria in spite of the observation that the gently sonicated mitochondria oxidized the 3-hydroxybutyryl-CoA much faster than the completely sonicated mitochondria. The NAD(+)-dependence of 3-hydroxybutyryl-CoA oxidation showed that a much smaller NAD+ concentration was enough to half-saturate the reaction in gently disrupted mitochondria than in completely disrupted ones. Thus, these observations indicate the positive kinetic consequence of organization of beta-oxidation enzymes in situ. Respiration-linked oxidation of butyryl-, octanoyl- and palmitoyl-CoA was also studied and these CoA intermediates were oxidized at approx. 50% of the rate of crotonyl- and 3-hydroxybutyryl-CoA in the gently disrupted mitochondria. In vigorously disrupted mitochondria the oxidation rate of these saturated acyl-CoA intermediates was hardly detectable indicating that the connection between the acyl-CoA dehydrogenase and the respiratory chain had been disrupted. | lld:pubmed |
| pubmed-article:1998730 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1998730 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1998730 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1998730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1998730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1998730 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1998730 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1998730 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:1998730 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:1998730 | pubmed:author | pubmed-author:AlkonyiII | lld:pubmed |
| pubmed-article:1998730 | pubmed:author | pubmed-author:SumegiBB | lld:pubmed |
| pubmed-article:1998730 | pubmed:author | pubmed-author:PorpaczyZZ | lld:pubmed |
| pubmed-article:1998730 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1998730 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:1998730 | pubmed:volume | 1081 | lld:pubmed |
| pubmed-article:1998730 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1998730 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1998730 | pubmed:pagination | 121-8 | lld:pubmed |
| pubmed-article:1998730 | pubmed:dateRevised | 2003-11-14 | lld:pubmed |
| pubmed-article:1998730 | pubmed:meshHeading | pubmed-meshheading:1998730-... | lld:pubmed |
| pubmed-article:1998730 | pubmed:meshHeading | pubmed-meshheading:1998730-... | lld:pubmed |
| pubmed-article:1998730 | pubmed:meshHeading | pubmed-meshheading:1998730-... | lld:pubmed |
| pubmed-article:1998730 | pubmed:meshHeading | pubmed-meshheading:1998730-... | lld:pubmed |
| pubmed-article:1998730 | pubmed:meshHeading | pubmed-meshheading:1998730-... | lld:pubmed |
| pubmed-article:1998730 | pubmed:meshHeading | pubmed-meshheading:1998730-... | lld:pubmed |
| pubmed-article:1998730 | pubmed:meshHeading | pubmed-meshheading:1998730-... | lld:pubmed |
| pubmed-article:1998730 | pubmed:meshHeading | pubmed-meshheading:1998730-... | lld:pubmed |
| pubmed-article:1998730 | pubmed:meshHeading | pubmed-meshheading:1998730-... | lld:pubmed |
| pubmed-article:1998730 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1998730 | pubmed:articleTitle | Kinetic advantage of the interaction between the fatty acid beta-oxidation enzymes and the complexes of the respiratory chain. | lld:pubmed |
| pubmed-article:1998730 | pubmed:affiliation | University Medical School, Institute of Biochemistry, Pecs, Hungary. | lld:pubmed |
| pubmed-article:1998730 | pubmed:publicationType | Journal Article | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1998730 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1998730 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1998730 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1998730 | lld:pubmed |
