Abstract
Polyclonal antibodies were raised against peptides corresponding to residues 1–15, 469–483 and 933–951 of the rabbit skeletal muscle L-type calcium channelα 2/δ primary translation product, for use as topological probes. Immunocytochemical comparison of the abilities of the antibodies to bind to theα 2 and δ subunits in intact and detergent-permeabilised rat dorsal root ganglion cells enabled the membrane orientation of these regions to be established. The resultant data indicate that the regions containing residues 1–15 and 469–483 of theα 2 subunit, and residues 1–17 of the δ subunit, are exposed on the extracellular surface of the membrane, findings consistent with a model that proposesα 2 to be entirely extracellular.
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