Separation by liquid chromatography (under elevated pressure) of benzyl and nitrophenyl glycosides of oligosaccharides

A galactose-binding lectin (galaptin) from human spleen has been purified to homogeneity by affinity chromatography on asialofetuin-Sepharose. The carbohydrate-binding specificity of galaptin has been investigated by analyzing the binding of galaptin to asialofetuin in the presence of putative inhibitors. An enzyme-linked immunosorbent assay (ELISA) was developed that involved adsorption of asialofetuin to microtiter plates. Galaptin bound to asialofetuin was detected with polyclonal rabbit anti-galaptin serum followed by goat anti-rabbit IgG-peroxidase conjugate. The concentrations of inhibitors giving 50% inhibition of galaptin binding relative to controls were graphically determined and normalized relative to galactose or lactose. These analyses revealed that galaptin has a combining site at least as large as a disaccharide. The disaccharides having non-reducing-terminal beta-galactosyl residues linked (1,3), (1,4), and (1,6) to Glc or GlcNAc are better inhibitors than free Gal. GalNAc, either free or glycosidically linked, appears to have no affinity for the lectin. The nitrophenyl galactosides are better inhibitors than methyl galactosides, indicating the occurrence of hydrophobic interactions. The data indicate that OH groups at C-4 and C-6 of Gal and the OH at C-3 of GlcNAc in Gal beta(1,4)GlcNAc are important for lectin sugar interaction. Our data support the hypothesis that endogenous receptors for galaptin are most likely lactosaminoglycan moieties.

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Use of Synthetic H Disaccharides as Acceptors for Detecting Activities of UDP-GalNAc:Fuc α1-->2Galβ-R α1-->3-N-Acetylgalactosaminyltransferase in Plasma Samples from Blood Group A Subgroups

Yazawa

Takeya

Hosomi

et al. 1992

Clinical Chemistry

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Concentrations of blood group A-specified alpha(1-->3)-N-acetylgalactosaminyltransferase (A enzyme) were measured in human plasma of blood groups A1, A2, and A3 by using chemically synthesized H disaccharides and H type 1 and type 2 trisaccharides attached to hydrophobic aglycones as acceptors. When the trisaccharides were used as acceptors, enzyme activities were reduced in samples from A2 and A3. However, the H disaccharides were shown to be good acceptors even for enzymes from A2 and A3, and no significant difference in enzyme concentration was detected in any of the plasma tested.

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Separation by liquid chromatography (under elevated pressure) of benzyl and nitrophenyl glycosides of oligosaccharides

Cited by 4 publications

References 35 publications

Transglycosylation and transfer reaction activities of endo-α-N-acetyl-D-galactosaminidase from Diplococcus (Streptococcus) pneumoniae

Transglycosylation and transfer reaction activities of endo-α-N-acetyl-D-galactosaminidase from Diplococcus (Streptococcus) pneumoniae

Human splenic galaptin: carbohydrate-binding specificity and characterization of the combining site

Use of Synthetic H Disaccharides as Acceptors for Detecting Activities of UDP-GalNAc:Fuc α1-->2Galβ-R α1-->3-N-Acetylgalactosaminyltransferase in Plasma Samples from Blood Group A Subgroups

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Separation by liquid chromatography (under elevated pressure) of benzyl and nitrophenyl glycosides of oligosaccharides

Cited by 4 publications

References 35 publications

Transglycosylation and transfer reaction activities of endo-α-N-acetyl-D-galactosaminidase from Diplococcus (Streptococcus) pneumoniae

Transglycosylation and transfer reaction activities of endo-α-N-acetyl-D-galactosaminidase from Diplococcus (Streptococcus) pneumoniae

Human splenic galaptin: carbohydrate-binding specificity and characterization of the combining site

Use of Synthetic H Disaccharides as Acceptors for Detecting Activities of UDP-GalNAc:Fuc α1--&gt;2Galβ-R α1--&gt;3-N-Acetylgalactosaminyltransferase in Plasma Samples from Blood Group A Subgroups

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Use of Synthetic H Disaccharides as Acceptors for Detecting Activities of UDP-GalNAc:Fuc α1-->2Galβ-R α1-->3-N-Acetylgalactosaminyltransferase in Plasma Samples from Blood Group A Subgroups