Glycoprotein Structure Determination by Mass Spectrometry

Author:

Dell Anne1,Morris Howard R.1

Affiliation:

1. Department of Biochemistry, Imperial College of Science, Technology and Medicine, London SW7 2AY, UK.

Abstract

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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4. In mammals this core fucose is linked to the 6-position of the GlcNAc whereas in plants it occurs at the 3-position. Invertebrates are capable of fucosylating the core at either or both positions and in rare instances a third fucose can be attached to the distal GlcNAc of the core (60).

5. Immunogenic glycoconjugates implicated in parasitic nematode diseases

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