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  Affinity labelling and identification of the high-affinity choline carrier from synaptic membranes of Torpedo electromotor nerve terminals with [3H]choline mustard.

Rylett, R. (1988). Affinity labelling and identification of the high-affinity choline carrier from synaptic membranes of Torpedo electromotor nerve terminals with [3H]choline mustard. Journal of Neurochemistry, 51(6), 1942-1945. doi:10.1111/j.1471-4159.1988.tb01182.x.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-2E57-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-2E59-D
Genre: Journal Article

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 Creators:
Rylett, R.J.1, Author              
Affiliations:
1Abteilung Neurochemie, MPI for biophysical chemistry, Max Planck Society, ou_578555              

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 Abstract: The physiological mechanisms regulating activity of the sodium-dependent, high-affinity choline transporter and the molecular events in the translocation process remain unclear; the protein has not been purified or characterized biochemically. In the present study, [3H]choline mustard aziridinium ion ([3H]ChM Az), a nitrogen mustard analogue of choline, bound irreversibly to presynaptic plasma membranes from Torpedo electric organ in a hemicholinium-sensitive, and sodium-, time-, and temperature-dependent manner. Specific binding of this ligand was greatest when it was incubated with membranes in the presence of sodium at 30°C. Separation of the 3H-labelled membrane proteins by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed that most of the radiolabel was associated with a polypeptide of apparent molecular mass of ∼42,000 daltons; labelling of this species was abolished in membranes incubated with ligand in the presence of HC-3. Two other 3H-labelled polypeptides were detected, with apparent molecular masses of ∼58,000 and 90,000 daltons; radiolabelling of the former was also HC-3 sensitive. [3H]ChM Az may be a useful affinity ligand in the purification of the choline carrier from cholinergic neurons.

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Language(s): eng - English
 Dates: 1988-12
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Journal of Neurochemistry
Source Genre: Journal
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Pages: - Volume / Issue: 51 (6) Sequence Number: - Start / End Page: 1942 - 1945 Identifier: -