David Hage

David Hage

David Hage
James Hewett University Professor of Chemistry

Department of Chemistry
University of Nebraska–Lincoln
704 Hamilton Hall
Lincoln, Nebraska 68588-0304
Office: 402-472-2744

Research Interests

Analytical chemistry, bioanalytical chemistry, analytical separation methods, high-performance liquid chromatography, capillary electrophoresis, affinity-based separations, affinity mass spectrometry, monolithic supports and hybrid separation media, affinity microcolumns and miniaturized separation systems, separation-based studies of biological interactions, analytical methods for personalized medicine, chromatographic immunoassays, immobilization methods for biochemicals

Selected Publications

  1. (1) Sobansky, M.R.; Hage, D.S. "Identification and analysis of stereoselective drug interactions with low density lipoprotein by high-performance affinity chromatography", Anal. Biochem. Chem. 2012;403;563-71.
  2. (2) Matsuda, R.; Anguizola, J.; Joseph, K.S.; Hage, D.S. "High-performance affinity chromatography and the analysis of drug interactions with modified proteins: binding of gliclazide with glycated human serum albumin", Anal. Bioanal. Chem. 2011;401;2811-19.
  3. (3) Barnaby, O.S.; Cerny, R.L.; Clarke, W.; Hage, D.S. "Quantitative analysis of glycation patterns in human serum albumin Using 16O/18O-labeling and MALDI-TOF MS", Clin. Chim. Acta 2011;412;1606-15.
  4. (4) Tong, Z.; Hage, D.S. "Characterization of interaction kinetics between chiral solutes and human serum albumin by using high-performance affinity chromatography and peak profiling", J. Chromatogr. A 2011;1218;6892-7.
  5. (5) Hage, D.S.; Anguizola, J.A.; Jackson, A.J.; Matsuda, R.; Papastavros, E.; Pfaunmiller, E.; Tong, Z.; Vargas-Badilla, J.; Yoo, M.J.; Zheng, X. "Chromatographic analysis of drug interactions in the serum proteome", Anal. Methods 2011;3;1449-60.
  6. (6) Yoo, M.J.; Hage, D.S. "High-throughput analysis of drug dissociation from serum proteins using affinity silica monoliths", J. Sep. Sci. 2011;34;2255-63.