All potential glycosylation sites of the nicotinic acetylcholine receptor δ subunit from Torpedo californica are utilized

Abstract

All possible N‐glycosylation sites of the δ subunit of the nicotinic acetylcholine receptor from Torpedo californica electric tissue are utilized. By a combination of microsequencing and mass spectrometry, it was shown that a high‐mannose‐type oligosaccharide is bound at Asn143 of the δ subunit. The oligosaccharides at positions Asn70 and Asn208 of the δ subunit are probably of the complex type. The utilized glycosylation sites pose restrictions on possible transmembrane folding models of the subunit. Copyright © 1994, Wiley Blackwell. All rights reserved