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Skip to Search Results- 20Electrospray ionization mass spectrometry
- 12Affinity
- 10Carbohydrates
- 9Complexes
- 6Binding
- 6Mass-spectrometry
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Comparative study of substrate and product binding to the human ABO(H) blood group glycosyltransferases
Download2009
Klassen, John S., Shoemaker, Glen K., Palcic, Monica M., Soya, Naoto
The first comparative thermodynamic study of the human blood group glycosyltransferases, α-(1→3)-N-acetylgalactosaminyltransferase (GTA) and α-(1→3)-galactosyltransferase (GTB), interacting with donor substrates, donor and acceptor analogs, and trisaccharide products in vitro is reported. The...
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Identifying nonspecific ligand binding in electrospray ionization mass spectrometry using the reporter molecule method
Download2009
Sun, Nian, Klassen, John S., Kitova, Elena N., Sun, Jiangxiao
The application of the reporter molecule (Mrep) method for identifying nonspecific complexes in the ES-MS analysis of protein-ligand and DNA-ligand interactions in vitro is described. To test the reliability of the method, it was applied to the ES-MS analysis of protein-carbohydrate complexes...
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Comparative study of substrate and product binding to the human ABO(H) blood group glycosyltransferases
Download2009
Shoemaker, Glen K., Klassen, John S., Palcic, Monica M., Soya, Naoto
The first comparative thermodynamic study of the human blood group glycosyltransferases, α-(1→3)-N-acetylgalactosaminyltransferase (GTA) and α-(1→3)-galactosyltransferase (GTB), interacting with donor substrates, donor and acceptor analogs, and trisaccharide products in vitro is reported. The...
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Nonspecific interactions between proteins and charged biomolecules in electrospray ionization mass spectrometry
Download2010
Soya, Naoto, Klassen, John S., Kitova, Elena N., Sun, Nian
An investigation of the nonspecific association of small charged biomolecules and proteins in electrospray ionization mass spectrometry (ES-MS) is described. Aqueous solutions containing pairs of proteins and a small acidic or basic biomolecule that does not interact specifically with either of...
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Nonspecific interactions between proteins and charged biomolecules in electrospray ionization mass spectrometry
Download2010
Kitova, Elena N., Sun, Nian, Klassen, John S., Soya, Naoto
An investigation of the nonspecific association of small charged biomolecules and proteins in electrospray ionization mass spectrometry (ES-MS) is described. Aqueous solutions containing pairs of proteins and a small acidic or basic biomolecule that does not interact specifically with either of...
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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-fatty acid interactions using electrospray ionization mass spectrometry
Download2011
Liu, Lan, Kitova, Elena N., Klassen, John S.
The application of the direct electrospray ionization mass spectrometry (ESI-MS) assay to quantify interactions between bovine β-lactoglobulin (Lg) and a series of fatty acids (FA), CH3(CH2)xCOOH, where x = 6 (caprylic acid, CpA), 8 (capric acid, CA), 10 (lauric acid, LA), 12 (myristic acid, MA),...
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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...