Biochemical Journal · 1989 · 27 citations · 13 references
Life SciencesBiochemistryCell BiologyCell BiophysicsIntracellular TransportMembrane BiophysicsElectrolyte HomeostasisIon PermeationLysosomal TransportPlasma Membrane OrganizationSodium Channel BiophysicsSodium HomeostasisBinding CapacityPlasma Membrane PermeabilizationPlasma Membrane Stabilization
Ouabain binding was studied in Xenopus laevis oocytes permeabilized by detergents. The behaviour of markers showed that 10 microM-digitonin selectively disrupts the plasma membrane. In the presence of ATP, oocytes permeabilized at 10 microM-digitonin bound no more ouabain molecules than were required to abolish active 86Rb+ uptake in the intact cells. However, the ouabain binding capacity increased approx. 2-fold when inner membranes were disrupted by SDS or excess digitonin, as judged from the accompanying release of the lysosomal marker beta-hexosaminidase. The results suggest that oocytes have a large internal pool of functional sodium pumps.
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Membrane insertion of alpha- and beta-subunits of Na+,K+-ATPase.
K. Geering, David I. Meyer, M P Paccolat et al. · Journal of Biological Chemistry · 1985 · 82 citations · Full text