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Glycobiology ProtocolsStructural Determination of O-Glycans by Tandem Mass Spectrometry

Glycobiology Protocols: Structural Determination of O-Glycans by Tandem Mass Spectrometry [Trans-sialidase (TS; E.C. 3.2.1.18) catalyzes the transfer of preferably α2,3-linked sialic acid to another glycan or glycoconjugate, forming a new α2,3-linkage to galactose or N-acetylgalactosamine. In the absence of an appropriate acceptor, TS acts as a sialidase, hydrolytically releasing glycosidically linked sialic acid. Interest in TS has increased rapidly in recent years owing to its great relevance to the pathogenicity of trypanosomes and its possible application in the regiospecific synthesis of sialylated carbohydrates and glycoconjugates. Recently, the authors described a newly developed nonradioactive screening test for monitoring TS activity (1). In this highly sensitive and specific assay, 4-methylumbelliferyl-β-D-galactoside is used as acceptor substrate and sialyllactose as donor to fluorimetrically detect enzyme activity in the low mU range (∼0.1–1 mU/mL possible). The test can be applied to screen a large number of samples quickly and reliably during enzyme purification, for testing inhibitors, and for monitoring TS activity during the production of monoclonal antibodies (2).] http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png

Glycobiology ProtocolsStructural Determination of O-Glycans by Tandem Mass Spectrometry

Part of the Methods in Molecular Biology Book Series (volume 347)
Editors: Brockhausen, Inka
Glycobiology Protocols — Jan 1, 2007

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References (12)

Publisher
Humana Press
Copyright
© Humana Press 2007
ISBN
978-1-58829-553-8
Pages
109 –123
DOI
10.1385/1-59745-167-3:109
Publisher site
See Chapter on Publisher Site

Abstract

[Trans-sialidase (TS; E.C. 3.2.1.18) catalyzes the transfer of preferably α2,3-linked sialic acid to another glycan or glycoconjugate, forming a new α2,3-linkage to galactose or N-acetylgalactosamine. In the absence of an appropriate acceptor, TS acts as a sialidase, hydrolytically releasing glycosidically linked sialic acid. Interest in TS has increased rapidly in recent years owing to its great relevance to the pathogenicity of trypanosomes and its possible application in the regiospecific synthesis of sialylated carbohydrates and glycoconjugates. Recently, the authors described a newly developed nonradioactive screening test for monitoring TS activity (1). In this highly sensitive and specific assay, 4-methylumbelliferyl-β-D-galactoside is used as acceptor substrate and sialyllactose as donor to fluorimetrically detect enzyme activity in the low mU range (∼0.1–1 mU/mL possible). The test can be applied to screen a large number of samples quickly and reliably during enzyme purification, for testing inhibitors, and for monitoring TS activity during the production of monoclonal antibodies (2).]

Published: Jan 1, 2007

Keywords: Sialic Acid; GlcNAc Residue; Electrospray Tandem Mass Spectrometry; Linked Sialic Acid; Acetylneuraminic Acid

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