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1 Laboratory of General Biochemistry, University of Chile, Santiago, Chile
The use of Rb86 as an analog of K+ was studied in human red cells and in brain cortex slices. In these systems, the uptake of Rb+ was found to follow saturation kinetics. It was demonstrated in red cells that K+ ions produce an inhibition of the competitive type on the uptake of Rb+, a requirement when two substances are transported by the same carrier. Furthermore, the values found for the K1 for K+ and for the Vmax for Rb+ are similar to those described in the literature for the Km(K+) and the Vmax(K+), respectively. Rubidium ions activated the efflux of Na22 from red cells and this effect, as well as the influx of Rb+1 itself, was inhibited by ouabain. In agreement with what has been reported by other authors for K+, sodium ions in the extracellular medium inhibited the uptake of Rb+ when the latter was present in low concentrations (0.2 mM). At higher concentrations of Rb+ (4 mM), Na+ activates the Rb+ uptake. Only part of the Na+-activated influx of Rb+ is inhibited by onabain. The possibility of an influx of Rb+ through pump lB and II is discussed. On the basis of these results it is coneluded that at least 90% of the Rb+ is transported in red cells through mechanisms that have the same characteristics as those that have been described for K+. In rat brain slices, Rb+ was actually accumulated up to 15 times in the tissue. In the presence of ouabain, the intracellular concentration of Rb+ reached a concentration equal to that in the incubation medium. The data presented indicate that Rb86 can be used as an analog of K42 in these systems.
Submitted on December 23, 1969