Difference between revisions of "Chinopoulos 2009"
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{{Publication | {{Publication | ||
|title=Chinopoulos Christos, Vajda Szilvia, Csanady, Laszlo, Mandi Miklos, Mathe Katalin, Adam-Vizi Vera (2009) A Novel Kinetic Assay of Mitochondrial ATP-ADP Exchange Rate Mediated by the ANT. Biophys J 96, 2490-504. | |title=Chinopoulos Christos, Vajda Szilvia, Csanady, Laszlo, Mandi Miklos, Mathe Katalin, Adam-Vizi Vera (2009) A Novel Kinetic Assay of Mitochondrial ATP-ADP Exchange Rate Mediated by the ANT. Biophys J 96, 2490-504. | ||
|info=https://pubmed.ncbi.nlm.nih.gov/19289073-a-novel-kinetic-assay-of-mitochondrial-atp-adp-exchange-rate-mediated-by-the-ant/?from_term=chinopoulos+magnesium+green&from_pos=3 | |info=[https://pubmed.ncbi.nlm.nih.gov/19289073-a-novel-kinetic-assay-of-mitochondrial-atp-adp-exchange-rate-mediated-by-the-ant/?from_term=chinopoulos+magnesium+green&from_pos=3 PMID: 24391134] | ||
|authors=Chinopoulos Christos, Vajda Szilvia, Csanady, Laszlo, Mandi Miklos, Mathe Katalin, Adam-Vizi Vera | |authors=Chinopoulos Christos, Vajda Szilvia, Csanady, Laszlo, Mandi Miklos, Mathe Katalin, Adam-Vizi Vera | ||
|year=2009 | |year=2009 | ||
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|mipnetlab=HU Budapest Chinopoulos C | |mipnetlab=HU Budapest Chinopoulos C | ||
}} | }} | ||
::::» Fluorometry protocol for [[Magnesium green]] | |||
{{Labeling | {{Labeling | ||
|enzymes=Adenine nucleotide translocase | |enzymes=Adenine nucleotide translocase | ||
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|additional=MgG, Safranin, ANT, | |additional=MgG, Safranin, ANT, | ||
}} | }} | ||
Revision as of 12:56, 5 March 2020
Chinopoulos Christos, Vajda Szilvia, Csanady, Laszlo, Mandi Miklos, Mathe Katalin, Adam-Vizi Vera (2009) A Novel Kinetic Assay of Mitochondrial ATP-ADP Exchange Rate Mediated by the ANT. Biophys J 96, 2490-504. |
Chinopoulos Christos, Vajda Szilvia, Csanady, Laszlo, Mandi Miklos, Mathe Katalin, Adam-Vizi Vera (2009) Biophys J
Abstract: A novel method exploiting the differential affinity of ADP and ATP to Mg(2+) was developed to measure mitochondrial ADP-ATP exchange rate. The rate of ATP appearing in the medium after addition of ADP to energized mitochondria, is calculated from the measured rate of change in free extramitochondrial [Mg2+] reported by the membrane-impermeable 5K+ salt of the Mg2+-sensitive fluorescent indicator, Magnesium Green, using standard binding equations. The assay is designed such that the adenine nucleotide translocase (ANT) is the sole mediator of changes in [Mg2+] in the extramitochondrial volume, as a result of ADP-ATP exchange. We also provide data on the dependence of ATP efflux rate within the 6.8-7.8 matrix pH range as a function of membrane potential. Finally, by comparing the ATP-ADP steady-state exchange rate to the amount of the ANT in rat brain synaptic, brain nonsynaptic, heart and liver mitochondria, we provide molecular turnover numbers for the known ANT isotypes.
• Keywords: Adenine nucleotide translocase, ANT, ATP-ADP exchange, Magnesium Green
• Bioblast editor: Cardoso Luiza HD,
• O2k-Network Lab: HU Budapest Chinopoulos C
- » Fluorometry protocol for Magnesium green
Labels:
Enzyme: Adenine nucleotide translocase Regulation: ADP, ATP, ATP production
MgG, Safranin, ANT