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Competitive inhibition of phlorizin binding byd-glucose and the influence of sodium: a study on isolated brush border membrane of rat kidney

MPS-Authors
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Frasch,  Werner
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Frohnert,  Peter P.
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Bode,  Folkert
Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society;

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Baumann,  Karl
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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引用

Frasch, W., Frohnert, P. P., Bode, F., Baumann, K., & Kinne, R. (1970). Competitive inhibition of phlorizin binding byd-glucose and the influence of sodium: a study on isolated brush border membrane of rat kidney. Pflügers Archiv: European Journal of Physiology, 320(3), 265-284. doi:10.1007/BF00587458.


引用: https://hdl.handle.net/21.11116/0000-0008-CD58-F
要旨
Glucose binding to the luminal cell membrane was studied in the isolated brush border of rat renal cortex by means of inhibition of phlorizin binding to a specific receptor site. This effect was reversible and stereospecific and fulfilled the criteria of fully competitive inhibition. Thus, the kinetic parameters of D-glucose binding to the same receptor could be derived. The affinity of the receptor to either substrate, phlorizin as well as D-glucose, increased with rising ambient sodium concentration while the number of binding sites remained unchanged. Other cations (K+, Ca++, Mg++) showed no effect on either parameter. The results of this study are in agreement with a model of transmembrane transport of glucose put forward by Crane.