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Article ; Online: Measuring Binding Constants of His-Tagged Proteins Using Affinity Chromatography and Ni-NTA Immobilized Enzymes.

Moser, Annette C / White, Benjamin / Kovacs, Frank A

Methods in molecular biology (Clifton, N.J.)

2020 Volume 2178, Page(s) 405–416

Abstract: Affinity chromatography is one way to measure the binding constants of a protein-ligand interaction. Here, we describe a method of measuring a binding constant using Ni-NTA resin to immobilize a His-tagged enzyme and the method of frontal analysis. While ...

Abstract	Affinity chromatography is one way to measure the binding constants of a protein-ligand interaction. Here, we describe a method of measuring a binding constant using Ni-NTA resin to immobilize a His-tagged enzyme and the method of frontal analysis. While other methods of immobilization are possible, using the strong affinity interaction between His-tagged proteins and Ni-NTA supports results in a fast, easy, and gentle method of immobilization. Once the affinity support is created, frontal analysis can be used to measure the binding constant between the protein and various analytes.
MeSH term(s)	Chromatography, Affinity ; Histidine/chemistry ; Histidine/genetics ; Nickel/chemistry ; Recombinant Fusion Proteins/chemistry ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/isolation & purification
Chemical Substances	Recombinant Fusion Proteins ; polyhistidine (26062-48-6) ; Histidine (4QD397987E) ; Nickel (7OV03QG267)
Language	English
Publishing date	2020-10-31
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-0716-0775-6_26
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Studies of antibody-antigen interactions by capillary electrophoresis: A review.

Moser, Annette C / Trenhaile, Sidney / Frankenberg, Kati

Methods (San Diego, Calif.)

2018 Volume 146, Page(s) 66–75

Abstract: Antibody-antigen interactions are vital in immunoassay development and can determine detection limits and analysis times. Capillary electrophoresis (CE) is a powerful technique that can be used to quantify antibody-antigen interactions. These CE methods ... ...

Abstract	Antibody-antigen interactions are vital in immunoassay development and can determine detection limits and analysis times. Capillary electrophoresis (CE) is a powerful technique that can be used to quantify antibody-antigen interactions. These CE methods range from simple separations of a premixed antibody and antigen sample applied as a short plug to allow for separation of complex, free antibody, and free antigen to more complex systems which inject complexed samples in the presence of antibody or antigen; or even injections of antibody and antigen sequentially. The objective of this review is to identify and describe various CE techniques which have been used to study antibody-antigen interactions. A brief discussion of linear and nonlinear curve fitting is also included.
MeSH term(s)	Antigen-Antibody Reactions ; Electrophoresis, Capillary/history ; Electrophoresis, Capillary/methods ; History, 20th Century ; History, 21st Century
Language	English
Publishing date	2018-03-15
Publishing country	United States
Document type	Historical Article ; Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	1066584-5
ISSN	1095-9130 ; 1046-2023
ISSN (online)	1095-9130
ISSN	1046-2023
DOI	10.1016/j.ymeth.2018.03.006
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Article: Studies of antibody-antigen interactions by capillary electrophoresis: A review

Moser, Annette C / Kati Frankenberg / Sidney Trenhaile

Methods. 2018 Aug. 15, v. 146

2018

Abstract	Antibody-antigen interactions are vital in immunoassay development and can determine detection limits and analysis times. Capillary electrophoresis (CE) is a powerful technique that can be used to quantify antibody-antigen interactions. These CE methods range from simple separations of a premixed antibody and antigen sample applied as a short plug to allow for separation of complex, free antibody, and free antigen to more complex systems which inject complexed samples in the presence of antibody or antigen; or even injections of antibody and antigen sequentially. The objective of this review is to identify and describe various CE techniques which have been used to study antibody-antigen interactions. A brief discussion of linear and nonlinear curve fitting is also included.
Keywords	antibodies ; antigen-antibody reactions ; antigens ; capillary electrophoresis ; immunoassays
Language	English
Dates of publication	2018-0815
Size	p. 66-75.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1066584-5
ISSN	1095-9130 ; 1046-2023
ISSN (online)	1095-9130
ISSN	1046-2023
DOI	10.1016/j.ymeth.2018.03.006
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Measuring binding constants of His-tagged proteins using affinity chromatography and Ni-NTA-immobilized enzymes.

Moser, Annette C / White, Benjamin / Kovacs, Frank A

Methods in molecular biology (Clifton, N.J.)

2014 Volume 1129, Page(s) 423–434

Abstract: Affinity chromatography is one way to measure the binding constants of a protein-ligand interaction. Here we describe a method of measuring a binding constant using Ni-NTA resin to immobilize a His-tagged enzyme and the method of frontal analysis. While ... ...

Abstract	Affinity chromatography is one way to measure the binding constants of a protein-ligand interaction. Here we describe a method of measuring a binding constant using Ni-NTA resin to immobilize a His-tagged enzyme and the method of frontal analysis. While other methods of immobilization are possible, using the strong affinity interaction between His-tagged proteins and Ni-NTA supports results in a fast, easy, and gentle method of immobilization. Once the affinity support is created, frontal analysis can be used to measure the binding constant between the protein and various analytes.
MeSH term(s)	Chromatography, Affinity/methods ; Enzymes, Immobilized/chemistry ; Enzymes, Immobilized/metabolism ; Histidine/chemistry ; Nickel/chemistry ; Proteins/chemistry ; Proteins/metabolism
Chemical Substances	Enzymes, Immobilized ; Proteins ; Histidine (4QD397987E) ; Nickel (7OV03QG267)
Language	English
Publishing date	2014
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-62703-977-2_30
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Immunoaffinity chromatography: an introduction to applications and recent developments.

Moser, Annette C / Hage, David S

Bioanalysis

2010 Volume 2, Issue 4, Page(s) 769–790

Abstract: Immunoaffinity chromatography (IAC) combines the use of LC with the specific binding of antibodies or related agents. The resulting method can be used in assays for a particular target or for purification and concentration of analytes prior to further ... ...

Abstract	Immunoaffinity chromatography (IAC) combines the use of LC with the specific binding of antibodies or related agents. The resulting method can be used in assays for a particular target or for purification and concentration of analytes prior to further examination by another technique. This review discusses the history and principles of IAC and the various formats that can be used with this method. An overview is given of the general properties of antibodies and of antibody-production methods. The supports and immobilization methods used with antibodies in IAC and the selection of application and elution conditions for IAC are also discussed. Several applications of IAC are considered, including its use in purification, immunodepletion, direct sample analysis, chromatographic immunoassays and combined analysis methods. Recent developments include the use of IAC with CE or MS, ultrafast immunoextraction methods and the use of immunoaffinity columns in microanalytical systems.
MeSH term(s)	Animals ; Antibodies, Immobilized/chemistry ; Antibodies, Immobilized/immunology ; Antibody Formation ; Binding, Competitive ; Chromatography, Affinity/methods ; Humans ; Immunoassay/methods
Chemical Substances	Antibodies, Immobilized
Language	English
Publishing date	2010-07-12
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ISSN	1757-6199
ISSN (online)	1757-6199
DOI	10.4155/bio.10.31
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Article ; Online: Clinical applications of capillary electrophoresis based immunoassays.

Moser, Annette C / Willicott, Corey W / Hage, David S

Electrophoresis

2013 Volume 35, Issue 7, Page(s) 937–955

Abstract: Immunoassays have long been an important set of tools in clinical laboratories for the detection, diagnosis, and treatment of disease. Over the last two decades, there has been growing interest in utilizing CE as a means for conducting immunoassays with ... ...

Abstract	Immunoassays have long been an important set of tools in clinical laboratories for the detection, diagnosis, and treatment of disease. Over the last two decades, there has been growing interest in utilizing CE as a means for conducting immunoassays with clinical samples. The resulting method is known as a CE immunoassay. This approach makes use of the selective and strong binding of antibodies for their targets, as is employed in a traditional immunoassay, and combines this with the speed, efficiency, and small sample requirements of CE. This review discusses the variety of ways in which CE immunoassays have been employed with clinical samples. An overview of the formats and detection modes that have been employed in these applications is first presented. A more detailed discussion is then given on the type of clinical targets and samples that have been measured or studied by using CE immunoassays. Particular attention is given to the use of this method in the fields of endocrinology, pharmaceutical measurements, protein and peptide analysis, immunology, infectious disease detection, and oncology. Representative applications in each of these areas are described, with these examples involving work with both traditional and microanalytical CE systems.
MeSH term(s)	Animals ; Electrophoresis, Capillary/methods ; Humans ; Immunoassay/methods
Language	English
Publishing date	2013-11-27
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	619001-7
ISSN	1522-2683 ; 0173-0835
ISSN (online)	1522-2683
ISSN	0173-0835
DOI	10.1002/elps.201300421
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Article: Capillary electrophoresis-based immunoassays: principles and quantitative applications.

Moser, Annette C / Hage, David S

Electrophoresis

2008 Volume 29, Issue 16, Page(s) 3279–3295

Abstract: The use of CE as a tool to conduct immunoassays has been an area of increasing interest over the last decade. This approach combines the efficiency, small sample requirements, and relatively high speed of CE with the selectivity of antibodies as binding ... ...

Abstract	The use of CE as a tool to conduct immunoassays has been an area of increasing interest over the last decade. This approach combines the efficiency, small sample requirements, and relatively high speed of CE with the selectivity of antibodies as binding agents. This review examines the various assay formats and detection modes that have been reported for these assays, along with some representative applications. Most CE immunoassays in the past have employed homogeneous methods in which the sample and reagents are allowed to react in solution. These homogeneous methods have been conducted as both competitive binding immunoassays and as noncompetitive binding immunoassays. Fluorescent labels are most commonly used for detection in these assays, but enzyme labels have also been utilized for such work. Some additional work has been performed in CE immunoassays with heterogeneous methods in which either antibodies or an analog of the analyte is immobilized to a solid support. These heterogeneous methods can be used for the selective isolation of analytes prior to their separation by CE or to remove a given species from a sample/reagent mixture prior to analysis by CE. These CE immunoassays can be used with a variety of detection modes, such as fluorescence, UV/Vis absorbance, chemiluminescence, electrochemical measurements, MS, and surface plasmon resonance.
MeSH term(s)	Electrophoresis, Capillary/instrumentation ; Electrophoresis, Capillary/methods ; Fluorescence ; Immunoassay/instrumentation ; Immunoassay/methods ; Luminescent Measurements/instrumentation ; Luminescent Measurements/methods
Language	English
Publishing date	2008-07-16
Publishing country	Germany
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	619001-7
ISSN	1522-2683 ; 0173-0835
ISSN (online)	1522-2683
ISSN	0173-0835
DOI	10.1002/elps.200700871
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Article ; Online: Biointeraction analysis of immobilized antibodies and related agents by high-performance immunoaffinity chromatography.

Pfaunmiller, Erika / Moser, Annette C / Hage, David S

Methods (San Diego, Calif.)

2011 Volume 56, Issue 2, Page(s) 130–135

Abstract: A method is described based on high-performance immunoaffinity chromatography for examining the interactions of immobilized antibodies or related binding agents with their targets. It is shown how this method can be used to obtain information on the ... ...

Abstract	A method is described based on high-performance immunoaffinity chromatography for examining the interactions of immobilized antibodies or related binding agents with their targets. It is shown how this method can be used to obtain information on the binding, elution and regeneration kinetics of immobilized binding agents, such as those used with immunoaffinity supports. The theory behind this approach is briefly described and it is demonstrated how both the kinetic and thermodynamic properties of a biointeraction can be determined experimentally through this method. Several applications are used to illustrate this technique, including antibody-antigen interactions and the binding of aptamers with their targets in the presence of silica-based supports. The same approach can be adapted for use with other types of targets, binding agents and support materials.
MeSH term(s)	2,4-Dichlorophenoxyacetic Acid/chemistry ; Adsorption ; Antibodies, Immobilized/analysis ; Antibodies, Immobilized/chemistry ; Antibody Affinity ; Antigen-Antibody Complex/analysis ; Antigen-Antibody Complex/chemistry ; Antigens/analysis ; Antigens/chemistry ; Atrazine/chemistry ; Chromatography, Affinity/instrumentation ; Chromatography, Affinity/methods ; Immunoassay/instrumentation ; Immunoassay/methods ; Kinetics ; Ligands ; Thermodynamics
Chemical Substances	Antibodies, Immobilized ; Antigen-Antibody Complex ; Antigens ; Ligands ; 2,4-Dichlorophenoxyacetic Acid (2577AQ9262) ; Atrazine (QJA9M5H4IM)
Language	English
Publishing date	2011-09-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1066584-5
ISSN	1095-9130 ; 1046-2023
ISSN (online)	1095-9130
ISSN	1046-2023
DOI	10.1016/j.ymeth.2011.08.016
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Article ; Online: Electromyography of pelvic floor muscles with true differential versus faux differential electrode configuration.

Ballmer, Claudia / Eichelberger, Patric / Leitner, Monika / Moser, Helene / Luginbuehl, Helena / Kuhn, Annette / Radlinger, Lorenz

International urogynecology journal

2020 Volume 31, Issue 10, Page(s) 2051–2059

Abstract: Introduction and hypothesis: In pelvic floor muscle (PFM) electromyography (EMG) two different bipolar configurations are applied: "true differential" configuration (TD) measures neuromuscular activity with two ipsilateral electrodes, whereas "faux ... ...

Abstract	Introduction and hypothesis: In pelvic floor muscle (PFM) electromyography (EMG) two different bipolar configurations are applied: "true differential" configuration (TD) measures neuromuscular activity with two ipsilateral electrodes, whereas "faux differential" configuration (FD) has two electrodes placed on each side of the PFMs. The aim of the study was to determine possible differences and the relationship between both configurations. Methods: A secondary data analysis of 28 continent (CON) and 22 stress urinary incontinent (SUI) women was performed. Surface EMG was measured using a vaginal probe during maximal voluntary (MVC) and fast voluntary (FVC) contractions. TD and FD were explored with amplitude- and time-related EMG parameters, cross-correlation coefficients (R(0)) and statistical parametric mapping (SPM). Results: Of a total of 62 comparisons of EMG parameters of MVC and FVC, only one comparison showed significant differences between the two configurations (CON group, FVC Conclusions: The findings suggest that TD and FD might measure neuromuscular activity almost the same. Very high cross-correlation coefficients and a very limited number of significant results from EMG parameters, as well as SPM, suggest that in the measured sample the choice of TD or FD might remain practically irrelevant. To gain further insight into the scientific and clinical relevance of choosing either of the electrode configurations, the comparisons should be re-evaluated on a sample with more severe incontinence symptoms.
MeSH term(s)	Electrodes ; Electromyography ; Female ; Humans ; Muscle Contraction ; Pelvic Floor ; Urinary Incontinence, Stress
Language	English
Publishing date	2020-02-17
Publishing country	England
Document type	Journal Article
ZDB-ID	1050631-7
ISSN	1433-3023 ; 0937-3462
ISSN (online)	1433-3023
ISSN	0937-3462
DOI	10.1007/s00192-020-04225-4
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Article: Biointeraction analysis of immobilized antibodies and related agents by high-performance immunoaffinity chromatography

Pfaunmiller, Erika / Moser, Annette C / Hage, David S

Methods. 2012 Feb., v. 56, no. 2

2012

Abstract	A method is described based on high-performance immunoaffinity chromatography for examining the interactions of immobilized antibodies or related binding agents with their targets. It is shown how this method can be used to obtain information on the binding, elution and regeneration kinetics of immobilized binding agents, such as those used with immunoaffinity supports. The theory behind this approach is briefly described and it is demonstrated how both the kinetic and thermodynamic properties of a biointeraction can be determined experimentally through this method. Several applications are used to illustrate this technique, including antibody–antigen interactions and the binding of aptamers with their targets in the presence of silica-based supports. The same approach can be adapted for use with other types of targets, binding agents and support materials.
Keywords	antibodies ; antigen-antibody reactions ; binding agents ; immunoaffinity chromatography ; oligonucleotides ; thermodynamics
Language	English
Dates of publication	2012-02
Size	p. 130-135.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1066584-5
ISSN	1095-9130 ; 1046-2023
ISSN (online)	1095-9130
ISSN	1046-2023
DOI	10.1016/j.ymeth.2011.08.016
Database	NAL-Catalogue (AGRICOLA)

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