All potential glycosylation sites of the nicotinic acetylcholine receptor delta subunit from Torpedo californica are utilized.
All possible N-glycosylation sites of the delta 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 delta subunit. The oligosaccharides at positions Asn70 and Asn208 of the delta subunit are probably of the complex type. The utilized glycosylation sites pose restrictions on possible transmembrane folding models of the subunit.
Strecker
A
A
Institut für Biochemie, Freie Universität Berlin, Germany.
Franke
P
P
Weise
C
C
Hucho
F
F
D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D006031:Glycosylation; D009682:Magnetic Resonance Spectroscopy; D013058:Mass Spectrometry; D008562:Membrane Glycoproteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D011978:Receptors, Nicotinic / Q000737:chemistry*; D014101:Torpedo
D008562:Membrane Glycoproteins; D011978:Receptors, Nicotinic