scholarly journals γ-Cyclodextrin Increases Hydrolysis of Gangliosides by Sialidase from Arthrobacter ureafaciens: Hydrolysis of Gangliosides

2009 ◽  
Vol 2009 ◽  
pp. 1-4 ◽  
Author(s):  
Rie Mitsumori ◽  
Tomohisa Kato ◽  
Kenichi Hatanaka
Keyword(s):  
Sialic Acid ◽  
Bile Salts ◽  
Ganglioside Gm1 ◽  
Terminal Sialic Acid ◽  
Hydrolysis Of ◽  
Asialo Gm1

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.

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
Keyword(s):  
Sialic Acid ◽  
Phosphotungstic Acid ◽  
Glycosidic Bond ◽  
Selective Hydrolysis ◽  
Fetuin A ◽  
Keggin Type ◽  
Terminal Sialic Acid ◽  
Non Destructive ◽  
Hydrolysis Of

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.

scholarly journals The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Kenichi Kamata ◽  
Kenji Mizutani ◽  
Katsuya Takahashi ◽  
Roberta Marchetti ◽  
Alba Silipo ◽  
...  
Keyword(s):  
Immune System ◽  
Sialic Acid ◽  
Ligand Binding ◽  
Steric Hindrance ◽  
Sequence Similarity ◽  
Binding Assays ◽  
Subunit Interface ◽  
Nmr Techniques ◽  
And Control ◽  
Asialo Gm1

AbstractSeviL is a recently isolated lectin found to bind to the linear saccharides of the ganglioside GM1b (Neu5Ac$$\alpha$$ α (2-3)Gal$$\beta$$ β (1-3)GalNAc$$\beta$$ β (1-4)Gal$$\beta$$ β (1-4)Glc) and its precursor, asialo-GM1 (Gal$$\beta$$ β (1-3)GalNAc$$\beta$$ β (1-4)Gal$$\beta$$ β (1-4)Glc). The crystal structures of recombinant SeviL have been determined in the presence and absence of ligand. The protein belongs to the $$\beta$$ β -trefoil family, but shows only weak sequence similarity to known structures. SeviL forms a dimer in solution, with one binding site per subunit, close to the subunit interface. Molecular details of glycan recognition by SeviL in solution were analysed by ligand- and protein-based NMR techniques as well as ligand binding assays. SeviL shows no interaction with GM1 due to steric hindrance with the sialic acid branch that is absent from GM1b. This unusual specificity makes SeviL of great interest for the detection and control of certain cancer cells, and cells of the immune system, that display asialo-GM1.

Identity of the activator proteins for the enzymatic hydrolysis of sulfatide, ganglioside GM1, and globotriaosylceramide

1987 ◽  
Vol 259 (2) ◽  
pp. 627-638 ◽  
Author(s):  
A. Vogel ◽  
W. Fürst ◽  
M.A. Abo-Hashish ◽  
M. Lee-Vaupel ◽  
E. Conzelmann ◽  
...  
Keyword(s):  
Enzymatic Hydrolysis ◽  
Ganglioside Gm1 ◽  
Activator Proteins ◽  
Hydrolysis Of

scholarly journals Kinetic studies on the acid hydrolysis of the methyl ketoside of unsubstituted and O-acetylated N-acetylneuraminic acid

1973 ◽  
Vol 133 (4) ◽  
pp. 623-628 ◽  
Author(s):  
A. Neuberger ◽  
Wendy A. Ratcliffe
Keyword(s):  
Sialic Acid ◽  
Acid Hydrolysis ◽  
Model Compound ◽  
Kinetic Studies ◽  
Order Rate Constant ◽  
Neuraminic Acid ◽  
Acetylneuraminic Acid ◽  
Rate Of Hydrolysis ◽  
Ph Range ◽  
Hydrolysis Of

The hydrolysis of the model compound 2-O-methyl-4,7,8,9-tetra-O-acetyl-N-acetyl-α-d-neuraminic acid and neuraminidase (Vibrio cholerae) closely resembled that of the O-acetylated sialic acid residues of rabbit Tamm–Horsfall glycoprotein. This confirmed that O-acetylation was responsible for the unusually slow rate of acid hydrolysis of O-acetylated sialic acid residues observed in rabbit Tamm–Horsfall glycoprotein and their resistance to hydrolysis by neuraminidase. The first-order rate constant of hydrolysis of 2-methyl-N-acetyl-α-d-neuraminic acid by 0.05m-H2SO4 was 56-fold greater than that of 2-O-methyl-4,7,8,9-tetra-O-acetyl-N-acetyl -α-d-neuraminic acid. Kinetic studies have shown that in the pH range 1.00–3.30, the observed rate of hydrolysis of 2-methyl-N-acetyl-α-d-neuraminic acid can be attributed to acid-catalysed hydrolysis of the negatively charged CO2− form of the methyl ketoside.

Sialic Acid Content And The Biological Activity Of Stuart Factor (F X)

1981 ◽  
Author(s):  
A M Engel
Keyword(s):  
Biological Activity ◽  
Sialic Acid ◽  
Sodium Citrate ◽  
Complete Removal ◽  
Maximal Activity ◽  
Disc Electrophoresis ◽  
Sialic Acid Content ◽  
Activation System ◽  
Hydrolysis Of ◽  
Esterase Activities

Substantial release of sialic acid (SA) from purified F X was obtained with sialidase from Clostridium perfringens. The total SA content of F X was found to be 1.7%, in agreement with previous reports. After almost complete removal of SA, aliquots were examined by polyacrilamide disc electrophoresis and by polyacrilamide in sodium dodecy1 sulphate (SDS) and the gels were stained for proteins and for glycoproteins. When SA was progressively removed from F X its clotting activity was slightly increased while its electrophoretic mobility was retarded, as expected. The tryptic activation of F X was affected by the removal of 60-70% of SA, yielding more clotting activity than the native F X. No difference was observed between the esterase activity of regular F X and asialo-X as measured by the hydrolysis of N-alpha-acetyl glycyl-L-lysy1-methyl ester acetate (AGLMe).When asialo-X was interacted with 25% sodium citrate the kinetics were accelerated and the maximal clotting and esterase activities were obtained at 6 hours of activation while the native F X reached the peack of both activities at 24 hours. Both activation mixtures were analyzed, at the period of maximal activity, for liberation of peptidic material by thin-layer electrophoresis (TLE). TLE patterns of asialo-X varied according to the activation system used; they also differed from the ones obtained with native F X.The data indicate that SA influences the kinetic of activation of F X and the nature and distribution of the peptidic material released during activation.

scholarly journals Utilization of Ganglioside-Degrading Paenibacillus sp. Strain TS12 for Production of Glucosylceramide

2002 ◽  
Vol 68 (11) ◽  
pp. 5241-5248 ◽  
Author(s):  
Tomomi Sumida ◽  
Noriyuki Sueyoshi ◽  
Makoto Ito
Keyword(s):  
Sialic Acid ◽  
Cellular Differentiation ◽  
Bovine Brain ◽  
New Method ◽  
Degrading Enzymes ◽  
Bacterial Enzyme ◽  
Paenibacillus Sp ◽  
Brain Gangliosides ◽  
Asialo Gm1

ABSTRACT Gangliosides, sialic acid-containing glycosphingolipids, are membrane constituents of vertebrates and are known to have important roles in cellular differentiation, adhesion, and recognition. We report here the isolation of a bacterium capable of degrading gangliotetraose-series gangliosides and a new method for the production of glucosylceramide with this bacterium. GM1a ganglioside was found to be sequentially degraded by Paenibacillus sp. strain TS12, which was isolated from soil, as follows: GM1a → asialo GM1 → asialo GM2 → lactosylceramide → glucosylceramide. TS12 was found to produce a series of ganglioside-degrading enzymes, such as sialidases, β-galactosidases, and β-hexosaminidases. TS12 also produced β-glucosidases, but glucosylceramide was somewhat resistant to the bacterial enzyme under the conditions used. Taking advantage of the specificity, we developed a new method for the production of glucosylceramide using TS12 as a biocatalyst. The method involves the conversion of crude bovine brain gangliosides to glucosylceramide by coculture with TS12 and purification of the product by chromatography with Wakogel C-300 HG.

THE EFFECT OF PH AND BILE SALTS ON THE HYDROLYSIS OF A SELF-EMULSIFIED SYSTEM BY PANCREATIC LIPASE

1990 ◽  
Vol 42 (S1) ◽  
pp. 134P-134P
Author(s):  
D. Challis ◽  
C.W. Pouton ◽  
B.J. Meakin ◽  
S.P. Jones
Keyword(s):  
Pancreatic Lipase ◽  
Bile Salts ◽  
Effect Of Ph ◽  
Hydrolysis Of
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