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Solubilization of ligand-stabilized vasopressin receptors from plasma membranes of bovine kidney and rat liver

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Boer,  Rainer
Department of Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Crause,  Peter
Department of Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Fahrenholz,  Falk
Department of Physical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Boer, R., Crause, P., & Fahrenholz, F. (1983). Solubilization of ligand-stabilized vasopressin receptors from plasma membranes of bovine kidney and rat liver. Biochemical and Biophysical Research Communications, 116(1), 91-98. doi:10.1016/0006-291X(83)90385-6.


Cite as: http://hdl.handle.net/21.11116/0000-0007-D4AB-9
Abstract
The solubilization of vasopressin receptors from plasma membranes of bovine kidney and rat liver by different detergents was investigated. A prerequisite for the extraction of vasopressin receptors retaining binding affinity for their ligand was the stabilization of the receptors by the prior formation of the membrane-bound hormone-receptor complexes. The vasopressin-receptor complexes from both kidney and liver membranes were solubilized in a high yield with dodecyl-β-D-maltoside and 3-laurylamido-N,N′-dimethylpropylaminoxide. Several other nonionic detergents including octyl-β-D-glucopyranoside effectively extracted the hepatic vasopressin receptor. For the hormone-receptor complex solubilized from bovine kidney with dodecyl-β-D-maltoside, a Stokes' radius of 5.8 nm was determined.