Search
Skip to Search Results- 18Klassen, John S.
- 14Kitova, Elena N.
- 4Han, Ling
- 4N. Kitova, Elena N.
- 2Cairo, Christopher W.
- 2Daneshfar, Rambod
- 12Affinity
- 6Binding
- 6Electrospray ionization mass spectrometry
- 4Electrospray ionization
- 4Proteins
- 2Affinities
-
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),...
-
Quantifying protein-fatty acid interactions using electrospray ionization mass spectrometry
Download2011
Klassen, John S., Kitova, Elena N., Liu, Lan
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),...
-
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...
-
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...
-
Screening anti-cancer drugs against tubulin using catch-and-release electrospray ionization mass spectrometry
Download2016
Kitova, Elena N., Klassen, John S., Winter, Philip, Tuszynski, Jack A., Darestani, Reza R.
Tubulin, which is the building block of microtubules, plays an important role in cell division. This critical role makes tubulin an attractive target for the development of chemotherapeutic drugs to treat cancer. Currently, there is no general binding assay for tubulin–drug interactions. The...
-
Screening anti-cancer drugs against tubulin using catch-and-release electrospray ionization mass spectrometry
Download2016
Kitova, Elena N., Klassen, John S., Winter, Philip, Tuszynski, Jack A., Darestani, Reza R.
Tubulin, which is the building block of microtubules, plays an important role in cell division. This critical role makes tubulin an attractive target for the development of chemotherapeutic drugs to treat cancer. Currently, there is no general binding assay for tubulin–drug interactions. The...
-
Screening oligosaccharide libraries against lectins using the proxy protein electrospray ionization mass spectrometry assay
Download2016
Kitova, Elena N., Klassen, John S., Fan, Xuxin, Privé, Gilbert G., Cairo, Christopher W., Xiong, Zi Jian, Ng, Kenneth K. S., Zou, Chunxia, Eugenio, Luiz, Li, Jun
An electrospray ionization mass spectrometry (ESI-MS) assay for screening carbohydrate libraries against lectins is described. The assay is based on the proxy protein ESI-MS method, which combines direct ESI-MS protein–ligand binding measurements and competitive protein binding, to simultaneously...
-
Screening oligosaccharide libraries against lectins using the proxy protein electrospray ionization mass spectrometry assay
Download2016
Privé, Gilbert G., Ng, Kenneth K. S., Xiong, Zi Jian, Klassen, John S., Kitova, Elena N., Fan, Xuxin, Li, Jun, Zou, Chunxia, Eugenio, Luiz, Cairo, Christopher W.
An electrospray ionization mass spectrometry (ESI-MS) assay for screening carbohydrate libraries against lectins is described. The assay is based on the proxy protein ESI-MS method, which combines direct ESI-MS protein–ligand binding measurements and competitive protein binding, to simultaneously...