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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1994-6-9
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pubmed:abstractText |
Saponin-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.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Flavoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Muscle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NADP,
http://linkedlifedata.com/resource/pubmed/chemical/Saponins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0003-2697
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
216
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
322-7
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8179187-Adenosine Diphosphate,
pubmed-meshheading:8179187-Female,
pubmed-meshheading:8179187-Flavoproteins,
pubmed-meshheading:8179187-Fluorescence,
pubmed-meshheading:8179187-Fluorometry,
pubmed-meshheading:8179187-Humans,
pubmed-meshheading:8179187-Middle Aged,
pubmed-meshheading:8179187-Mitochondria, Muscle,
pubmed-meshheading:8179187-Muscle Proteins,
pubmed-meshheading:8179187-Muscles,
pubmed-meshheading:8179187-NADP,
pubmed-meshheading:8179187-Oxidation-Reduction,
pubmed-meshheading:8179187-Oxidative Phosphorylation,
pubmed-meshheading:8179187-Saponins,
pubmed-meshheading:8179187-Spectrometry, Fluorescence
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pubmed:year |
1994
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pubmed:articleTitle |
Measurement of fluorescence changes of NAD(P)H and of fluorescent flavoproteins in saponin-skinned human skeletal muscle fibers.
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pubmed:affiliation |
Institut für Biochemie, Medizinische Akademie Magdeburg, Germany.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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