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Neuronal membranes of postsynaptic origin twofold enriched in acetylcholinesterase, muscarinic acetylcholinereceptor and (Na+/K+)-ATP-Phosphohydrolase, proteins associated with cholinergic nerve excitability, were prepared with yields between 60 and 75% from bovine caudate nucleus. On subfractionation of these membranes an additional twofold enrichment of the mentioned proteins is achieved in different subfractions. SDS-gradient gel electrophoresis shows that these subfractions have slightly different polypeptide compositions. Neuronal membranes of presynaptic origin on the other hand, prepared from purified synaptosomes, possess only small amounts of the mentioned proteins, showing no enrichment with respect to the homogenate. Solubilization of acetylcholinesterase with 1 M NaC1 as well as of muscarinic acetylcholinreceptor with 2 M NaC1 does not succeed. These proteins are therefore not solely bound by ionic forces to the isolated membranes from bovine caudate nucleus.
K P Ruess, and
M Liefländer, and
K H Herzog
January 1977,
Biochemical Society transactions,
K P Ruess, and
M Liefländer, and
K H Herzog
February 1974,
European journal of pharmacology,
K P Ruess, and
M Liefländer, and
K H Herzog
September 1982,
Journal of neurochemistry,
K P Ruess, and
M Liefländer, and
K H Herzog
January 1977,
Acta biologica et medica Germanica,
K P Ruess, and
M Liefländer, and
K H Herzog
August 1979,
Bratislavske lekarske listy,
K P Ruess, and
M Liefländer, and
K H Herzog
November 1971,
Journal of neurochemistry,
K P Ruess, and
M Liefländer, and
K H Herzog
September 1982,
Neurochemical research,
K P Ruess, and
M Liefländer, and
K H Herzog
April 2003,
Neurochemical research,
K P Ruess, and
M Liefländer, and
K H Herzog
January 1985,
Progress in neuro-psychopharmacology & biological psychiatry,
K P Ruess, and
M Liefländer, and
K H Herzog
August 1988,
Biochemical Society transactions,
