ATTEMPTS TO ENRICH AND TO SOLUBILIZE THE MUSCARINIC ACETYLCHOLINE-RECEPTOR FROM BOVINE CAUDATE-NUCLEUS

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  • 1 January 1979
    • journal article
    • research article
    • Vol. 34  (1-2) , 51-59
Abstract
Neuronal membranes of postsynaptic origin enriched 2-fold in acetylcholinesterase, muscarinic acetylcholine receptor and (Na+/K+)-ATP-phosphohydrolase, proteins associated with cholinergic nerve excitability, were prepared with yields between 60-75% from bovine caudate nucleus. On subfractionation of these membranes an additional 2-fold enrichment of the mentioned proteins is achieved in different subfractions. SDS[sodium dodecyl sulfate]-gradient gel electrophoresis shows that these subfractions have slightly different polypeptide compositions. Neuronal membranes of presynaptic origin prepared from purified synaptosomes, possess only small amounts of these proteins, showing no enrichment with respect to the homogenate. Solubilization of acetylcholinesterase with 1 M NaCl and of muscarinic acetylcholine receptor with 2 M NaCl does not succeed. These proteins are not solely bound by ionic forces to the isolated membranes from bovine caudate nucleus.