Glycoprotein structure determination by mass spectrometry.
The human genome encodes 30,000 to 40,000 proteins, and a major challenge is to understand how posttranslational events, such as glycosylation, affect the activities and functions of these proteins in health and disease. Glycosylated proteins are ubiquitous components of extracellular matrices and cellular surfaces where their oligosaccharide moieties are implicated in a wide range of cell-cell and cell-matrix recognition events. The power of ultrahigh-sensitivity mass spectrometric strategies for defining the primary structures of highly complex mixtures of glycoprotein glycoforms is set to revolutionize structural glycobiology in the coming postgenomic era.
Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AY, UK. a.dell@ic.ac.uk
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D000818:Animals; D002239:Carbohydrate Metabolism, Inborn Errors / Q000378:metabolism; D005260:Female; D000071816:Glycodelin; D006023:Glycoproteins / Q000737:chemistry* / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods; D009077:Mucins / Q000737:chemistry; D011247:Pregnancy; D011257:Pregnancy Proteins / Q000737:chemistry / Q000378:metabolism; D011328:Prions / Q000737:chemistry / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D021241:Spectrometry, Mass, Electrospray Ionization; D016339:Spectrometry, Mass, Fast Atom Bombardment; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D000071816:Glycodelin; D006023:Glycoproteins; D009077:Mucins; C045246:PAEP protein, human; D011257:Pregnancy Proteins; D011328:Prions