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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1978-3-21
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pubmed:abstractText |
1. The use of 1,N6-ethenoadenosine 5'-triphosphate (epsilon-ATP), a synthetic, fluorescent analog of ATP, by whole rat liver mitochondria and by submitochondrial particles produced via sonication has been studied. 2. Direct [3H]adenine nucleotide uptake studies with isolated mitochondria, indicate the epsilon-[3H]ATP is not transported through the inner membrane by the adenine nucleotide carrier and is therefore not utilized by the 2,4-dinitrophenol-sensitive F1-ATPase (EC 3.6.1.3) that functions in oxidative phosphorylation. However, epsilon-ATP is hydrolyzed by a Mg2+-dependent, 2,4-dinitrophenol-insensitive ATPase that is characteristic of damaged mitochondria. 3. epsilon-ATP can be utilized quite well by the exposed F1-ATPase of sonic submitochondrial particles. This epsilon-ATP hydrolysis activity is inhibited by oligomycin and stimulated by 2,4-dinitrophenol. The particle F1-ATPase displays similar Km values for both ATP and epsilon-ATP; however, the V with ATP is approximately six times greater than with epsilon-ATP. 4. Since epsilon-ATP is a capable substrate for the submitochondrial particle F1-ATPase, it is proposed that the fluorescent properties of this ATP analog might be employed to study the submitochondrial particle F1-ATPase complex, and its response to various modifiers of oxidative phosphorylation.
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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 Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Dinitrophenols,
http://linkedlifedata.com/resource/pubmed/chemical/Ethenoadenosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Mitochondrial ADP, ATP Translocases,
http://linkedlifedata.com/resource/pubmed/chemical/Nucleotidyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Oligomycins
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
9
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pubmed:volume |
501
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
269-74
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:145875-Adenosine Triphosphatases,
pubmed-meshheading:145875-Adenosine Triphosphate,
pubmed-meshheading:145875-Animals,
pubmed-meshheading:145875-Biological Transport,
pubmed-meshheading:145875-Cell Fractionation,
pubmed-meshheading:145875-Dinitrophenols,
pubmed-meshheading:145875-Ethenoadenosine Triphosphate,
pubmed-meshheading:145875-Male,
pubmed-meshheading:145875-Mitochondria, Liver,
pubmed-meshheading:145875-Mitochondrial ADP, ATP Translocases,
pubmed-meshheading:145875-Nucleotidyltransferases,
pubmed-meshheading:145875-Oligomycins,
pubmed-meshheading:145875-Oxidative Phosphorylation,
pubmed-meshheading:145875-Rats,
pubmed-meshheading:145875-Substrate Specificity
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pubmed:year |
1978
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pubmed:articleTitle |
The extent of mitochondrial F1-ATPase and adenine nucleotide carrier activity with epsilon-ATP.
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pubmed:publicationType |
Journal Article
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