ATP-Mg/Pi carrier activity in rat liver mitochondria.
ATP-Mg/Pi carrier activity in rat liver mitochondria.
复制标题
大鼠肝线粒体中的 ATP-Mg/Pi 载体活性。
DOI:
10.1016/0003-9861(92)90628-a
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发表时间:
1992
影响因子:
3.9
通讯作者:
Aprille,JR
中科院分区:
文献类型:
--
作者:
Nosek,MT;Aprille,JR
Abstract The ATP-Mg P i carrier in liver mitochondria is activated by micromolar Ca 2+ and mediates net adenine nucleotide transport into and out of the mitochondrial matrix. The purpose of this study was to characterize certain features of ATP-Mg P i carrier activity that are essential for understanding how the mitochondrial adenine nucleotide content is regulated. The relative importance of ATP and ADP as transport substrates was investigated using specific trap assays to measure their separate rates of carrier-mediated efflux with P i as the external counterion. Under energized conditions ATP efflux accounted for 88% of total ATP+ ADP efflux. With oligomycin present to lower the matrix ATP ADP ratio, ATP efflux was eliminated and ADP efflux was relatively unaffected. Mg 2+ was stoichiometrically required for ATP influx and is probably transported simultaneously with ATP. Ca 2+ and Mn 2+ could substitute for the stoichiometric Mg 2+ requirement. ADP influx and P i-induced adenine nucleotide efflux were unaffected by external Mg 2+. Experiments with P i analogues suggested that P i is transported as the divalent anion, HPO 4 2−. The results show that ATP-Mg and divalent P i are the major transport substrates; the most probable transport mechanism for the ATP-Mg P i carrier is an electroneutral exchange. The results are consistent with the hypothesis that the direction and magnitude of net adenine nucleotide movements are determined mainly by the (ATP-Mg) 2− and HPO 4 2− concentration gradients across the inner mitochondrial membrane.