Structure of the glycosyl-phosphatidylinositol membrane anchor of acetylcholinesterase from the electric organ of the electric-fish, Torpedo californica

• Published in: Biochemical journal Vol. 296; no. 2; pp. 473 - 479
• Main Authors: MEHLERT, A, VARON, L, SILMAN, I, HOMANS, S. W, FERGUSON, M. A. J
• Format: Journal Article
• Language: English
• Published: Colchester Portland Press 01-12-1993
• Subjects: Acetylcholinesterase - chemistry; Acetylcholinesterase - isolation & purification; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Carbohydrate Conformation; Carbohydrate Sequence; Cell Membrane - enzymology; Electric Organ - enzymology; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Glycoside Hydrolases; Glycosylphosphatidylinositols - chemistry; Glycosylphosphatidylinositols - isolation & purification; Hydrolases; Magnetic Resonance Spectroscopy; Methylation; Molecular Sequence Data; Oligosaccharides - chemistry; Oligosaccharides - isolation & purification; Phosphatidylinositol Diacylglycerol-Lyase; Phosphoric Diester Hydrolases - metabolism; Torpedo; Vertebrata; Glycophospholipid; Enzyme; Pisces; Torpedo californica; Hydrolases; Esterases; Chemical composition; Acetylcholinesterase; Carbohydrate chain; Carboxylic ester hydrolases; Structural analysis
• ISSN: 0264-6021; 1470-8728
• DOI: 10.1042/bj2960473

The structure of the glycan moiety of the glycosyl-phosphatidylinositol (GPI) membrane anchor from Torpedo californica (electric fish) electric-organ acetylcholinesterase was solved using n.m.r., methylation analysis and chemical and enzymic micro-sequencing. Two structures were found to be present: Glc alpha 1-2Man alpha 1-2Man alpha 1-6Man alpha 1-4GlcN alpha 1-6myo-inositol and Glc alpha 1-2Man alpha 1-2Man alpha 1-6(GalNAc beta 1-4)Man alpha 1-4GlcN alpha 1-6myo-inositol. The presence of glucose in this GPI anchor structure is a novel feature. The anchor was also shown to contain 2.3 residues of ethanolamine per molecule.