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- W2000658356 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." @default.
- W2000658356 created "2016-06-24" @default.
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- W2000658356 creator A5088037931 @default.
- W2000658356 date "2009-03-01" @default.
- W2000658356 modified "2023-10-14" @default.
- W2000658356 title "A Novel Kinetic Assay of Mitochondrial ATP-ADP Exchange Rate Mediated by the ANT" @default.
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- W2000658356 doi "https://doi.org/10.1016/j.bpj.2008.12.3915" @default.
- W2000658356 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2907717" @default.
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