Polyoxometalates as sialidase mimics: selective and non-destructive removal of sialic acid from a glycoprotein promoted by phosphotungstic acid

2017 ◽  
Vol 53 (76) ◽  
pp. 10600-10603 ◽  
Author(s):  
Laura Sofia Van Rompuy ◽  
Tatjana N. Parac-Vogt

The selective hydrolysis of the glycosidic bond between the terminal sialic acid and the penultimate sugar has been achieved in the alpha-2-HS-glycoprotein (Fetuin-A) in the presence of H3PW12O40, a Keggin type polyoxometalate.

2013 ◽  
Vol 19 (8) ◽  
pp. 2848-2858 ◽  
Author(s):  
Karen Stroobants ◽  
Eva Moelants ◽  
Hong Giang T. Ly ◽  
Paul Proost ◽  
Kristin Bartik ◽  
...  

2020 ◽  
Vol 26 (69) ◽  
pp. 16463-16471
Author(s):  
Laura S. Van Rompuy ◽  
Jens Moons ◽  
Jo Aelbers ◽  
Tom Struyf ◽  
Wim Van den Ende ◽  
...  

2009 ◽  
Vol 2009 ◽  
pp. 1-4 ◽  
Author(s):  
Rie Mitsumori ◽  
Tomohisa Kato ◽  
Kenichi Hatanaka

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.


Cellulose ◽  
2016 ◽  
Vol 23 (2) ◽  
pp. 1199-1207 ◽  
Author(s):  
Dandan Qiang ◽  
Meiyun Zhang ◽  
Jinbao Li ◽  
Huijuan Xiu ◽  
Qiang Liu

2014 ◽  
Vol 11 (6) ◽  
pp. 684-689 ◽  
Author(s):  
Jing-Yuan LIU ◽  
He-Shui YU ◽  
Bing FENG ◽  
Li-Ping KANG ◽  
Xu PANG ◽  
...  

1997 ◽  
Vol 38 (17) ◽  
pp. 2981-2984 ◽  
Author(s):  
Véronique Le Boisselier ◽  
Michèle Postel ◽  
Elisabet Duñach

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