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Skip to Search Results- 12Klassen, John S.
- 10El-Hawiet, Amr
- 6Kitova, Elena N.
- 4N. Kitova, Elena N.
- 2Armstrong, Glen D.
- 2Daneshfar, Rambod
- 4Affinity
- 4Carbohydrates
- 4Electrospray ionization mass spectrometry
- 4Human milk oligosaccharide
- 4Library screening
- 4Toxin
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2011
Dingle, Tanis C., Szpacenko, Adam, Ng, Kenneth K.S., Kitov, Pavel, Klassen, John S., El-Hawiet, Amr, Kitova,Elena N., Mulvey, George L., Eugenio, Luiz, Armstrong, Glen D.
The binding of recombinant fragments of the C-terminal cell-binding domains of the two large exotoxins, toxin A (TcdA) and toxin B (TcdB), expressed by Clostridium difficile and a library consisting of the most abundant neutral and acidic human milk oligosaccharides (HMOs) was examined...
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2011
El-Hawiet, Amr, Klassen, John S., Armstrong, Glen D., Dingle, Tanis C., Eugenio, Luiz, Mulvey, George L., Szpacenko, Adam, Ng, Kenneth K.S., Kitova,Elena N., Kitov, Pavel
The binding of recombinant fragments of the C-terminal cell-binding domains of the two large exotoxins, toxin A (TcdA) and toxin B (TcdB), expressed by Clostridium difficile and a library consisting of the most abundant neutral and acidic human milk oligosaccharides (HMOs) was examined...
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Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry
Download2010
El-Hawiet, Amr, Klassen, John S., Kitova, Elena N., Liu, Lan
A new electrospray ionization mass spectrometry (ES-MS) approach for quantifying protein—ligand complexes that are prone to in-source (gas-phase) dissociation is described. The method, referred to here as the reference ligand ES-MS method, is based on the direct ES-MS assay and competitive ligand...
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Quantifying labile protein-ligand interactions using electrospray ionization mass spectrometry
Download2010
El-Hawiet, Amr, Liu, Lan, Klassen, John S., Kitova, Elena N.
A new electrospray ionization mass spectrometry (ES-MS) approach for quantifying protein—ligand complexes that are prone to in-source (gas-phase) dissociation is described. The method, referred to here as the reference ligand ES-MS method, is based on the direct ES-MS assay and competitive ligand...
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Quantifying protein-carbohydrate interactions using liquid sample desorption electrospray ionization mass spectrometry
Download2015
N. Kitova, Elena N., Shams-Ud-Doha, Km, Yao, Yuyu, Klassen, John S., Daneshfar, Rambod
The application of liquid sample desorption electrospray ionization mass spectrometry (liquid sample DESI-MS) for quantifying protein–carbohydrate interactions in vitro is described. Association constants for the interactions between lysozyme and β-D-GlcNAc-(1 → 4)-β-D-GlcNAc-(1 → 4)-D-GlcNAc and...
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Quantifying protein-carbohydrate interactions using liquid sample desorption electrospray ionization mass spectrometry
Download2015
Klassen, John S., N. Kitova, Elena N., Yao, Yuyu, Shams-Ud-Doha, Km, Daneshfar, Rambod
The application of liquid sample desorption electrospray ionization mass spectrometry (liquid sample DESI-MS) for quantifying protein–carbohydrate interactions in vitro is described. Association constants for the interactions between lysozyme and β-D-GlcNAc-(1 → 4)-β-D-GlcNAc-(1 → 4)-D-GlcNAc and...
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2015
El-Hawiet, Amr, N. Kitova, Elena N., Klassen, John S.
The affinities of the most abundant oligosaccharides found in human milk for four bacterial exotoxins (from Vibrio cholerae and pathogenic Escherichia coli) were quantified for the first time. Association constants (Ka) for a library of 20 human milk oligosaccharides (HMOs) binding to Shiga toxin...
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2015
El-Hawiet, Amr, Klassen, John S., N. Kitova, Elena N.
The affinities of the most abundant oligosaccharides found in human milk for four bacterial exotoxins (from Vibrio cholerae and pathogenic Escherichia coli) were quantified for the first time. Association constants (Ka) for a library of 20 human milk oligosaccharides (HMOs) binding to Shiga toxin...
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Reliable determinations of protein-ligand interactions by direct ESI-MS measurements: Are we there yet?
Download2012
El-Hawiet, Amr, Klassen, John S., Kitova, Elena N., Schnier, Paul D.
The association-dissociation of noncovalent interactions between protein and ligands, such as other proteins, carbohydrates, lipids, DNA, or small molecules, are critical events in many biological processes. The discovery and characterization of these interactions is essential to a complete...
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Reliable determinations of protein-ligand interactions by direct ESI-MS measurements: Are we there yet?
Download2012
Klassen, John S., Kitova, Elena N., Schnier, Paul D., El-Hawiet, Amr
The association-dissociation of noncovalent interactions between protein and ligands, such as other proteins, carbohydrates, lipids, DNA, or small molecules, are critical events in many biological processes. The discovery and characterization of these interactions is essential to a complete...