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Title: Aggregation and denaturation of antibodies: a capillary electrophoresis, dynamic light scattering, and aqueous two-phase partitioning study
Author (s): Bermudez, Ondrea
Forciniti, Daniel
Department/Lab Affiliations: Center for Environmental Science and Technology (CEST)
Chemical & Biological Engineering
Keywords: Aggregation
Aqueous two-phase systems
Denaturation
Dynamic light scattering
Immunoglobulin G
Partitioning
Issue Date: 2004-07-25
Publisher: Elsevier
Citation: Bermudez, Ondrea., and Forciniti, Daniel. "Aggregation and Denaturation of Antibodies: A Capillary Electrophoresis, Dynamic Light Scattering, and Aqueous Two-Phase Partitioning Study." Journal of Chromatography B, vol. 807, no. 1, pg 17-24, 2004.
Abstract: Protein denaturation and aggregation are well-known problems in the pharmaceutical industry. As the protein aggregates, it loses its biological activity and creates problems in its administration to patients. In this paper, we explore the use of aqueous two-phase systems, capillary zone electrophoresis, and dynamic light scattering for the monitoring of protein denaturation and aggregation. Our studies focus on human IgG and HSA. Capillary zone electrophoresis was used to monitor changes in the charge to size ratio of the proteins upon denaturation and dynamic light scattering was used to detect the presence of any aggregates and to monitor the size of the proteins. The information obtained from aqueous two-phase partitioning is similar to that obtained from capillary zone electrophoresis. The simplicity of aqueous two-phase system and its low cost (compared to the other analytical techniques) suggest that it can be routinely used for the quality control of some pharmaceutical preparations.
Type: Article - Journal
text
In Title: Journal of Chromatography B
Copyright Notice: This material is presented to ensure timely dissemination of scholarly and technical work. Copyright and all rights therein are retained by authors or by other copyright holders. All persons copying this information are expected to adhere to the terms and constraints invoked by each author's copyright. In most cases, these works may not be reposted without the explicit permission of the copyright holder.
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Publisher URL:
http://dx.doi.org/10.1016/j.jchromb.2004.01.029
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titleAggregation and denaturation of antibodies: a capillary electrophoresis, dynamic light scattering, and aqueous two-phase partitioning study
contributor.authorBermudez, Ondrea
contributor.authorForciniti, Daniel
contributor.deptlabCenter for Environmental Science and Technology (CEST)
contributor.deptlabChemical & Biological Engineering
subjectAggregation
subjectAqueous two-phase systems
subjectDenaturation
subjectDynamic light scattering
subjectImmunoglobulin G
subjectPartitioning
date.issued2004-07-25
publisherElsevier
identifier.citationBermudez, Ondrea., and Forciniti, Daniel. "Aggregation and Denaturation of Antibodies: A Capillary Electrophoresis, Dynamic Light Scattering, and Aqueous Two-Phase Partitioning Study." Journal of Chromatography B, vol. 807, no. 1, pg 17-24, 2004.
identifier.pub.URI
http://dx.doi.org/10.1016/j.jchromb.2004.01.029
description.abstractProtein denaturation and aggregation are well-known problems in the pharmaceutical industry. As the protein aggregates, it loses its biological activity and creates problems in its administration to patients. In this paper, we explore the use of aqueous two-phase systems, capillary zone electrophoresis, and dynamic light scattering for the monitoring of protein denaturation and aggregation. Our studies focus on human IgG and HSA. Capillary zone electrophoresis was used to monitor changes in the charge to size ratio of the proteins upon denaturation and dynamic light scattering was used to detect the presence of any aggregates and to monitor the size of the proteins. The information obtained from aqueous two-phase partitioning is similar to that obtained from capillary zone electrophoresis. The simplicity of aqueous two-phase system and its low cost (compared to the other analytical techniques) suggest that it can be routinely used for the quality control of some pharmaceutical preparations.
typeArticle - Journal
type.DCMITypetext
type.statusFinal version
rightsThis material is presented to ensure timely dissemination of scholarly and technical work. Copyright and all rights therein are retained by authors or by other copyright holders. All persons copying this information are expected to adhere to the terms and constraints invoked by each author's copyright. In most cases, these works may not be reposted without the explicit permission of the copyright holder.
rights.URI
http://www.elsevier.com/wps/find/authorsview.authors/authorsrights
relation.isPartOfJournal of Chromatography B
date.accessioned2007-04-11T17:00:48Z
date.available2008-05-30T19:19:46Z
identifier.persist.URI
http://scholarsmine.mst.edu/post_prints/AggregationAndDenaturationOfAntibodiesACapillar_09007dcc80502cc4.html