Journal
BIOPHYSICAL JOURNAL
Volume 96, Issue 6, Pages 2490-2504Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2008.12.3915
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Funding
- Semmelweis University Research Grant [63320]
- OTKA-NKTH [NF68294]
- OTKA
- MTA
- NKTH
- ETT
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A novel method exploiting the differential affinity of ADP and ATP to Mg2+ 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.
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