γ-Cyclodextrin Increases Hydrolysis of Gangliosides by Sialidase from Arthrobacter ureafaciens : Hydrolysis of Gangliosides
Joint Authors
Kato, Tomohisa
Mitsumori, Rie
Hatanaka, Kenichi
Source
International Journal of Carbohydrate Chemistry
Issue
Vol. 2009, Issue 2009 (31 Dec. 2009), pp.1-4, 4 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2009-02-02
Country of Publication
Egypt
No. of Pages
4
Main Subjects
Abstract EN
Sialidase is a ubiquitous enzyme that catalyzes the hydrolytic removal of terminal sialic acid residues from oligosaccharides in glycolipids and glycoproteins.
Ganglioside GM1 has been usually found to be resistant to various sialidases.
Arthrobacter ureafaciens sialidase has been reported to remove sialyl residues of ganglioside GM1 in the presence of bile salts.
However, bile salts are difficult to be removed, and disturb HPTLC analysis.
Using γ-cyclodextrin (γ-CD) as a novel additive agent, ganglioside GM1 was efficiently hydrolyzed to asialo-GM1 by A.
ureafaciens sialidase.
American Psychological Association (APA)
Mitsumori, Rie& Kato, Tomohisa& Hatanaka, Kenichi. 2009. γ-Cyclodextrin Increases Hydrolysis of Gangliosides by Sialidase from Arthrobacter ureafaciens : Hydrolysis of Gangliosides. International Journal of Carbohydrate Chemistry،Vol. 2009, no. 2009, pp.1-4.
https://search.emarefa.net/detail/BIM-469000
Modern Language Association (MLA)
Mitsumori, Rie…[et al.]. γ-Cyclodextrin Increases Hydrolysis of Gangliosides by Sialidase from Arthrobacter ureafaciens : Hydrolysis of Gangliosides. International Journal of Carbohydrate Chemistry No. 2009 (2009), pp.1-4.
https://search.emarefa.net/detail/BIM-469000
American Medical Association (AMA)
Mitsumori, Rie& Kato, Tomohisa& Hatanaka, Kenichi. γ-Cyclodextrin Increases Hydrolysis of Gangliosides by Sialidase from Arthrobacter ureafaciens : Hydrolysis of Gangliosides. International Journal of Carbohydrate Chemistry. 2009. Vol. 2009, no. 2009, pp.1-4.
https://search.emarefa.net/detail/BIM-469000
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-469000