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- W2011557714 abstract "The binding of [3H]-bumetanide to rat brain synaptosomes revealed the existence of two binding sites. The high affinity site (R1 = 46.6 moles/mg protein) binds bumetanide and furosemide with Kd1 of 13 nM and 1.5 μM respectively, while the low affinity site (R2 = 1.37 nmoles/mg protein) is characterized by Kd2 of 200 μM and 680 μM for bumetanide and furosemide, respectively. Bumetanide sensitive 86Rb uptake was 34+14.5, 38.3+1.4, 18.6+1.3 and 29.0+6.1% of total 86Rb uptake in synaptic plasma membrane vesicles, rat brain synaptosomes, Neuroblastoma N1E115 cell line and chick chest muscle cells, respectively. Furosemide and bumetanide inhibited 86Rb uptake to rat brain SPM- vesicles in a dose dependent fashion. Half maximal inhibition (IC50) was observed at 20 nM and 4 μM for bumetanide and furosemide, respectively. Bumetanide-sensitive transport was dependent on extravesicular sodium and chloride concentrations with a Km of 21 and 25 mM for the two ions, respectively. These results demonstrate the existence of a “loop diuretic” sensitive carrier-mediated K+ transport system in brain and other excitable cells." @default.
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- W2011557714 date "1989-01-01" @default.
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- W2011557714 title "A bumetanide-sensitive, potassium carrier-mediated transport system in excitable tissues" @default.
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- W2011557714 doi "https://doi.org/10.1016/0024-3205(89)90483-9" @default.
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