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Jeanethe Anguizola

University of Nebraska–Lincoln

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David S. Hage

University of Nebraska–Lincoln

Ryan Matsuda

University of Nebraska–Lincoln

Erika L. Pfaunmiller

University of Nebraska–Lincoln

Efthimia Papastavros

University of Nebraska–Lincoln

Xiwei Zheng

Harbin Medical University

Matthew Sobansky

University of Nebraska–Lincoln

Abby Jackson

University of Nebraska–Lincoln

K.S. Joseph

University of Nebraska–Lincoln

Cong Bi

Shandong Provincial Hospital

Mitchell L. Milanuk

University of Nebraska–Lincoln

Cooperative Institutions

University of Nebraska–Lincoln

Institute of Environmental Assessment and Water Research

University of Messina

Instituto de Investigación en Ciencias de la Alimentación

Università Campus Bio-Medico

Czech Academy of Sciences, Institute of Analytical Chemistry

Consejo Superior de Investigaciones Científicas

Pfizer (United States)

Tbilisi State University

Masaryk University

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Elsevier eBooks (2013)

A. Alfonso Jeanethe Anguizola ‪Damià Barceló Geoffrey S. Baird Kimber L. Barnett

10.1016/b978-0-12-415806-1.01002-0

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Chromatographic analysis of the effects of fatty acids and glycation on binding by probes for Sudlow sites I and II to human serum albumin

Journal of Chromatography B (2015)

Jeanethe Anguizola Erin DeBolt D. Suresh David S. Hage

Human serum albumin

Serum Albumin

Human albumin

10.1016/j.jchromb.2015.09.041

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Citations (14)

Chromatographic analysis of acetohexamide binding to glycated human serum albumin

Journal of Chromatography B (2010)

K.S. Joseph Jeanethe Anguizola Abby Jackson David S. Hage

Human serum albumin

Serum Albumin

10.1016/j.jchromb.2010.08.021

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Citations (55)

Use of protein G microcolumns in chromatographic immunoassays: A comparison of competitive binding formats

Journal of Chromatography B (2016)

Erika L. Pfaunmiller Jeanethe Anguizola Mitchell L. Milanuk NaTasha Carter David S. Hage

Competitive binding

Human serum albumin

Linear range

10.1016/j.jchromb.2015.12.055

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Citations (11)

Affinity chromatography

Elsevier eBooks (2023)

David S. Hage Jeanethe Anguizola Rong Li Ryan Matsuda Efthimia Papastavros

Ion chromatography

Affinity electrophoresis

10.1016/b978-0-323-99968-7.00034-5

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Citations (6)

Pharmaceutical and biomedical applications of affinity chromatography: Recent trends and developments

Journal of Pharmaceutical and Biomedical Analysis (2012)

David S. Hage Jeanethe Anguizola Cong Bi Rong Li Ryan Matsuda

Affinity electrophoresis

Ion chromatography

10.1016/j.jpba.2012.01.004

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Citations (198)

Affinity chromatographic studies of drug-protein binding in personalized medicine

Jeanethe Anguizola

Personalized Medicine

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Citations (1)

Studies of metabolite–protein interactions: A review

Journal of Chromatography B (2013)

Ryan Matsuda Cong Bi Jeanethe Anguizola Matthew Sobansky Elliott Rodriguez

Xenobiotic

10.1016/j.jchromb.2013.11.043

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Citations (38)

Development of Affinity Microcolumns for Drug–Protein Binding Studies in Personalized Medicine: Interactions of Sulfonylurea Drugs with in vivo Glycated Human Serum Albumin

Analytical Chemistry (2013)

Jeanethe Anguizola K.S. Joseph Omar Barnaby Ryan Matsuda Guadalupe Alvarado

This report used high-performance affinity microcolumns to examine the changes in binding by sulfonylurea drugs to in vivo glycated HSA that had been isolated from individual patients with diabetes. An immunoextraction approach was developed to isolate HSA and glycated HSA from clinical samples, using only 20 μL of plasma or serum and 6–12 nmol of protein to prepare each affinity microcolumn. It was found that the affinity microcolumns could be used in either frontal analysis or zonal elution studies, which typically required only 4–8 min per run. The microcolumns had good stability and allowed data to be obtained for multiple drugs and experimental conditions over hundreds of sample application cycles. Both the overall binding, as measured by frontal analysis, and site-specific interactions, as examined by zonal elution, showed good agreement with previous data that had been obtained for in vitro glycated HSA with similar levels of modification. It was also possible to directly compare the changes in site-specific binding that occurred between sulfonylurea drugs or as the level of HSA glycation was varied. This method is not limited to clinical samples of glycated HSA but could be adapted for work with other modified proteins of interest in personalized medicine.

Human serum albumin

Sulfonylurea

Binding affinities

Serum Albumin

10.1021/ac303734c

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Citations (68)

Peak decay analysis and biointeraction studies of immunoglobulin binding and dissociation on protein G affinity microcolumns

Jeanethe Anguizola Erika L. Pfaunmiller Mitchell L. Milanuk David S. Hage

Protein G

Protein A

Target protein

10.1016/j.ymeth.2018.03.013

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Citations (11)