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Isolation and reconstitution of the high‐affinity choline carrier
Author(s) -
Knipper M.,
Boekhoff I.,
Breer H.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80228-5
Subject(s) - choline , liposome , membrane , chemistry , monoclonal antibody , biochemistry , transporter , affinity chromatography , phosphatidyl choline , sodium , antibody , chromatography , biology , enzyme , phospholipid , organic chemistry , gene , immunology
Monoclonal antibodies, which block the high‐affinity uptake of choline in synaptosomal ghosts, have been used to purify a membrane polypeptide (80 kDa) from insect synaptosomal membranes. This isolated protein was found to catalyse the sodium‐dependent, hemicholinium‐sensitive accumulation of choline after reconstitution into liposomes, thus, apparently represents the high‐affinity choline transporter.

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