Statements in which the resource exists.
SubjectPredicateObjectContext
pubmed-article:8179187rdf:typepubmed:Citationlld:pubmed
pubmed-article:8179187lifeskim:mentionsumls-concept:C0086418lld:lifeskim
pubmed-article:8179187lifeskim:mentionsumls-concept:C1704336lld:lifeskim
pubmed-article:8179187lifeskim:mentionsumls-concept:C0016223lld:lifeskim
pubmed-article:8179187lifeskim:mentionsumls-concept:C0027270lld:lifeskim
pubmed-article:8179187lifeskim:mentionsumls-concept:C0242485lld:lifeskim
pubmed-article:8179187lifeskim:mentionsumls-concept:C0392747lld:lifeskim
pubmed-article:8179187lifeskim:mentionsumls-concept:C0016315lld:lifeskim
pubmed-article:8179187lifeskim:mentionsumls-concept:C0303920lld:lifeskim
pubmed-article:8179187pubmed:issue2lld:pubmed
pubmed-article:8179187pubmed:dateCreated1994-6-9lld:pubmed
pubmed-article:8179187pubmed:abstractTextSaponin-skinned human muscle fibers from M. vastus lateralis were immobilized in a quartz capillary to detect the fluorescence changes of NAD(P)H and of fluorescent flavoproteins. To get sufficient intense fluorescence signals from a small amount of muscle tissue the NAD(P)H fluorescence was excited by means of an HeCd laser at 325 nm and the flavoprotein fluorescence by an argon-ion laser at 454 nm or by the second wavelength of a HeCd laser at 442 nm. Using this experimental setup the fluorescence spectra of NAD(P)H, of alpha-lipoamide dehydrogenase and of electron-transfer flavoprotein were detected in saponin-skinned human muscle fibers. These fibers behaved identically to isolated mitochondria: (i) The addition of substrates caused an increase in reduction of mitochondrial NAD+, (ii) the addition of ADP caused its reoxidation, and (iii) the addition of respiratory chain inhibitors led to an almost complete reduction of NAD+. It was observed that the redox state of the NAD(P) system and of the alpha-lipoamide dehydrogenase reached after addition of 1 mM ADP correlates with the rate of active state respiration with NAD-dependent substrates. Therefore, this fluorimetric method is suitable to compare the mitochondrial oxidation capacities of NAD-dependent substrates in less then 5 mg wet weight muscle tissue. Moreover, the maximal changes in fluorescence of NAD(P)H and flavoproteins correlate with the amount of mitochondrial marker enzymes per milligram muscle tissue. Using this method a myopathy caused by a diminished content of mitochondria per milligram muscle tissue was observed.lld:pubmed
pubmed-article:8179187pubmed:languageenglld:pubmed
pubmed-article:8179187pubmed:journalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8179187pubmed:citationSubsetIMlld:pubmed
pubmed-article:8179187pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8179187pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8179187pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8179187pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8179187pubmed:chemicalhttp://linkedlifedata.com/r...lld:pubmed
pubmed-article:8179187pubmed:statusMEDLINElld:pubmed
pubmed-article:8179187pubmed:monthFeblld:pubmed
pubmed-article:8179187pubmed:issn0003-2697lld:pubmed
pubmed-article:8179187pubmed:authorpubmed-author:WinklerKKlld:pubmed
pubmed-article:8179187pubmed:authorpubmed-author:KuznetsovA...lld:pubmed
pubmed-article:8179187pubmed:authorpubmed-author:NeumannH WHWlld:pubmed
pubmed-article:8179187pubmed:authorpubmed-author:GellerichF...lld:pubmed
pubmed-article:8179187pubmed:authorpubmed-author:KunzW SWSlld:pubmed
pubmed-article:8179187pubmed:authorpubmed-author:NeuhofSSlld:pubmed
pubmed-article:8179187pubmed:issnTypePrintlld:pubmed
pubmed-article:8179187pubmed:day1lld:pubmed
pubmed-article:8179187pubmed:volume216lld:pubmed
pubmed-article:8179187pubmed:ownerNLMlld:pubmed
pubmed-article:8179187pubmed:authorsCompleteYlld:pubmed
pubmed-article:8179187pubmed:pagination322-7lld:pubmed
pubmed-article:8179187pubmed:dateRevised2006-11-15lld:pubmed
pubmed-article:8179187pubmed:meshHeadingpubmed-meshheading:8179187-...lld:pubmed
pubmed-article:8179187pubmed:meshHeadingpubmed-meshheading:8179187-...lld:pubmed
pubmed-article:8179187pubmed:meshHeadingpubmed-meshheading:8179187-...lld:pubmed
pubmed-article:8179187pubmed:meshHeadingpubmed-meshheading:8179187-...lld:pubmed
pubmed-article:8179187pubmed:meshHeadingpubmed-meshheading:8179187-...lld:pubmed
pubmed-article:8179187pubmed:meshHeadingpubmed-meshheading:8179187-...lld:pubmed
pubmed-article:8179187pubmed:meshHeadingpubmed-meshheading:8179187-...lld:pubmed
pubmed-article:8179187pubmed:meshHeadingpubmed-meshheading:8179187-...lld:pubmed
pubmed-article:8179187pubmed:meshHeadingpubmed-meshheading:8179187-...lld:pubmed
pubmed-article:8179187pubmed:meshHeadingpubmed-meshheading:8179187-...lld:pubmed
pubmed-article:8179187pubmed:meshHeadingpubmed-meshheading:8179187-...lld:pubmed
pubmed-article:8179187pubmed:meshHeadingpubmed-meshheading:8179187-...lld:pubmed
pubmed-article:8179187pubmed:meshHeadingpubmed-meshheading:8179187-...lld:pubmed
pubmed-article:8179187pubmed:meshHeadingpubmed-meshheading:8179187-...lld:pubmed
pubmed-article:8179187pubmed:meshHeadingpubmed-meshheading:8179187-...lld:pubmed
pubmed-article:8179187pubmed:year1994lld:pubmed
pubmed-article:8179187pubmed:articleTitleMeasurement of fluorescence changes of NAD(P)H and of fluorescent flavoproteins in saponin-skinned human skeletal muscle fibers.lld:pubmed
pubmed-article:8179187pubmed:affiliationInstitut für Biochemie, Medizinische Akademie Magdeburg, Germany.lld:pubmed
pubmed-article:8179187pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:8179187pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:8179187pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:8179187lld:pubmed
http://linkedlifedata.com/r...pubmed:referesTopubmed-article:8179187lld:pubmed