sodium-nitrite and 2--7--bis(carboxyethyl)-5(6)-carboxyfluorescein

sodium-nitrite has been researched along with 2--7--bis(carboxyethyl)-5(6)-carboxyfluorescein* in 1 studies

Other Studies

1 other study(ies) available for sodium-nitrite and 2--7--bis(carboxyethyl)-5(6)-carboxyfluorescein

Article	Year
Plasma membrane K+/H(+)-ATPase from Leishmania donovani. Journal of cellular physiology, 1994, Volume: 159, Issue:1 Leishmania donovani has an active K+/H+ exchange system on the surface membrane. Modulation of external K+ concentration resulted in a corresponding change in internal pH (pHi) suggesting a link between proton and potassium transport. Although a Na+/H+ antiporter is present on the plasma membrane, its sensitivity to amiloride suggests that it operates independent of K+/H+ exchange. Reduction of cellular ATP with NaN3 and KCN inhibits K+/H+ exchange showing thereby that the process is energy dependent. The K+/H+ exchange is sensitive to inhibitors of the gastric K+/H(+)-ATPase. It is concluded that the H(+)-ATPase previously reported on the plasma membrane of L. donovani is in fact a K+/H(+)-ATPase. Topics: Adenosine Triphosphate; Amiloride; Animals; Biological Transport; Cell Membrane; Fluoresceins; H(+)-K(+)-Exchanging ATPase; Hydrogen-Ion Concentration; Leishmania donovani; Nigericin; Potassium; Potassium Cyanide; Proton Pump Inhibitors; Sodium Nitrite	1994

Article

Year

Plasma membrane K+/H(+)-ATPase from Leishmania donovani.

Journal of cellular physiology, 1994, Volume: 159, Issue:1

Leishmania donovani has an active K+/H+ exchange system on the surface membrane. Modulation of external K+ concentration resulted in a corresponding change in internal pH (pHi) suggesting a link between proton and potassium transport. Although a Na+/H+ antiporter is present on the plasma membrane, its sensitivity to amiloride suggests that it operates independent of K+/H+ exchange. Reduction of cellular ATP with NaN3 and KCN inhibits K+/H+ exchange showing thereby that the process is energy dependent. The K+/H+ exchange is sensitive to inhibitors of the gastric K+/H(+)-ATPase. It is concluded that the H(+)-ATPase previously reported on the plasma membrane of L. donovani is in fact a K+/H(+)-ATPase.

Topics: Adenosine Triphosphate; Amiloride; Animals; Biological Transport; Cell Membrane; Fluoresceins; H(+)-K(+)-Exchanging ATPase; Hydrogen-Ion Concentration; Leishmania donovani; Nigericin; Potassium; Potassium Cyanide; Proton Pump Inhibitors; Sodium Nitrite

1994