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

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:...

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Bibliographic Details
Published in:Biochemical journal 1993-12, Vol.296 (2), p.473-479
Main Authors: MEHLERT, A, VARON, L, SILMAN, I, HOMANS, S. W, FERGUSON, M. A. J
Format: Article
Language:English
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
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Summary: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.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2960473