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Use of site‐directed antibodies to probe the topography of theα 2 subunit of voltage‐gated Ca 2+ channels
Author(s) -
Kieran Brickley,
Veronica A. Campbell,
Nicholas S. Berrow,
Robert Leach,
Robert I. Norman,
Dennis Wray,
Annette Dolphin,
Stephen A. Baldwin
Publication year - 1995
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(95)00371-f
Subject(s) - polyclonal antibodies , protein subunit , extracellular , dorsal root ganglion , chemistry , biophysics , immunocytochemistry , antibody , voltage gated ion channel , biochemistry , ion channel , dorsum , biology , anatomy , immunology , gene , endocrinology , receptor
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.