NR ATYV
AU Baldwin,M.A.
TI Analysis of glycosylphosphatidylinositol protein anchors: the prion protein.
QU Methods in Enzymology 2005; 405: 172-87
PT journal article; review
AB Membrane proteins constitute a substantial fraction of the human proteome. A small subgroup associates with membranes through the presence of a C-terminal lipid anchor that is joined to the protein via a phosphoglycan. The prion protein (PrP), an abnormally folded form that causes fatal neurodegeneration, is one example of a glycosylphosphatidylinositol (GPI)-anchored protein. Although GPI-anchored proteins were first recognized some 20 years ago (in the mid-1980s), relatively few GPI anchors have been analyzed in detail. Therefore, a description of the analysis of the PrP-GPI anchor using a variety of mass spectrometric methods is of interest even though some of the approaches adopted could be facilitated through the use of newer, more sensitive techniques.
ZR 22
MH Biochemistry/methods; Chromatography, High Pressure Liquid; Galactose/chemistry; Glycosylphosphatidylinositols/*chemistry; Inositol/chemistry; Lipids/chemistry; Mannose/chemistry; Models, Biological; Models, Chemical; N-Acetylneuraminic Acid/chemistry; Neurodegenerative Diseases/pathology; Oligosaccharides/chemistry; Peptides/chemistry; Polysaccharides/chemistry; Prions/*chemistry; Protein Structure, Tertiary; Proteomics/*methods; Spectrometry, Mass, Electrospray Ionization; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Spectrum Analysis, Mass/*methods; Time Factors
AD Mass Spectrometry Research Resource, Department of Pharmaceutical Chemistry, University of California, San Francisco, USA
SP englisch
PO USA