Temperature dependence of solute transport and enzyme activities in hog renal 
brush border membrane vesicles

De Smedt, H.; Kinne, Rolf

doi:10.1016/0005-2736(81)90040-7

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Temperature dependence of solute transport and enzyme activities in hog renal brush border membrane vesicles

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De Smedt, H.
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Kinne, Rolf
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

De Smedt, H., & Kinne, R. (1981). Temperature dependence of solute transport and enzyme activities in hog renal brush border membrane vesicles. Biochimica et Biophysica Acta-Biomembranes, 648(2), 247-253. doi:10.1016/0005-2736(81)90040-7.

Cite as: https://hdl.handle.net/21.11116/0000-0008-3E90-0

Abstract

The temperature dependence of sodium-dependent and sodium-independent D-glucose and phosphate uptake by renal brush border membrane vesicles has been studied under tracer exchange conditions. For sodium-dependent D-glucose and phosphate uptake, discontinuities in the Arrhenius plot were observed. The apparent activation energy for both processes increased at least 4-fold with decreasing temperature. The most striking change in the slope of the Arrhenius plot occurred between 12 and 15°C. The sodium-independent uptake of D-glucose and phosphate showed a linear Arrhenius plot over the temperature range tested (35–5°C). The behavior of the transport processes was compared to the temperature dependence of typical brush border membrane enzymes. Alkaline phosphatase as intrinsic membrane protein showed a nonlinear Arrhenius plot with a transition temperature at 12.4°C. Aminopeptidase M, an extrinsic membrane protein exhibited a linear Arrhenius plot. These data indicate that the sodium-glucose and sodium-phosphate cotransport systems are intrinsic brush border membrane proteins, and that a change in membrane organization alters the activity of a variety of intrinsic membrane proteins simultaneously.