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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 (6), 2490-504.
|title=Chinopoulos C, Vajda S, Csanady L, Mandi M, Mathe K, Adam-Vizi V (2009) A Novel Kinetic Assay of Mitochondrial ATP-ADP Exchange Rate Mediated by the ANT. Biophys J 96, 2490-504. doi:10.1016/j.bpj.2008.12.3915
|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/?from_single_result=A+Novel+Kinetic+Assay+of+Mitochondrial+ATP-ADP+Exchange+Rate+Mediated+by+the+ANT PMID: 24391134 Open Access]
|authors=Chinopoulos Christos, Vajda Szilvia, Csanady, Laszlo, Mandi Miklos, Mathe Katalin, Adam-Vizi Vera
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|authors=Chinopoulos Christos, Vajda Szilvia, Csanady Laszlo, Mandi Miklos, Mathe Katalin, Adam-Vizi Vera
|year=2009
|year=2009
|journal=Biophys J
|journal=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 [Mg(2+)] reported by the membrane-impermeable 5K(+) salt of the Mg(2+)-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 [Mg(2+)] 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.
|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 [Mg<sup>2+</sup>] reported by the membrane-impermeable 5K<sup>+</sup> salt of the Mg<sup>2+</sup>-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 [Mg<sup>2+</sup>] 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=ANT, ATP-ADP exchange, MgG
|keywords=Adenine nucleotide translocase, ANT, ATP-ADP exchange, Magnesium Green
|editor=[[Cardoso Luiza HD]],
|editor=[[Cardoso Luiza HD]],<br>
|mipnetlab=HU Budapest Chinopoulos C
|mipnetlab=HU Budapest Chinopoulos C
}}
}}
::::Β» Fluorometry protocol for [[Magnesium green]]
== Cited by ==
{{Template:Cited by Cardoso 2021 MitoFit MgG}}
{{Labeling
{{Labeling
|organism=Rat
|tissues=Heart, Nervous system, Liver
|preparations=Isolated mitochondria
|enzymes=Adenine nucleotide translocase
|enzymes=Adenine nucleotide translocase
|topics=ADP, ATP, ATP production
|topics=ADP, ATP, ATP production
|additional=MgG, Safranin, ANT,
|additional=MgG, Safranin, ANT, MitoFit 2021 MgG
}}
}}

Latest revision as of 10:52, 9 February 2022

Publications in the MiPMap
Chinopoulos C, Vajda S, Csanady L, Mandi M, Mathe K, Adam-Vizi V (2009) A Novel Kinetic Assay of Mitochondrial ATP-ADP Exchange Rate Mediated by the ANT. Biophys J 96, 2490-504. doi:10.1016/j.bpj.2008.12.3915

Β» PMID: 24391134 Open Access

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. β€’ Keywords: Adenine nucleotide translocase, ANT, ATP-ADP exchange, Magnesium Green β€’ Bioblast editor: Cardoso Luiza HD,
β€’ O2k-Network Lab: HU Budapest Chinopoulos C

Β» Fluorometry protocol for Magnesium green

Cited by

  • Cardoso et al (2021) Magnesium Green for fluorometric measurement of ATP production does not interfere with mitochondrial respiration. Bioenerg Commun 2021.1. doi:10.26124/bec:2021-0001


Labels:


Organism: Rat  Tissue;cell: Heart, Nervous system, Liver  Preparation: Isolated mitochondria  Enzyme: Adenine nucleotide translocase  Regulation: ADP, ATP, ATP production 



MgG, Safranin, ANT, MitoFit 2021 MgG