Recycling isotachophoresis: A novel approach to preparative protein fractionation

Persistent Link:
http://hdl.handle.net/10150/291469
Title:
Recycling isotachophoresis: A novel approach to preparative protein fractionation
Author:
Sloan, Jeffrey Edward, 1963-
Issue Date:
1987
Publisher:
The University of Arizona.
Rights:
Copyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.
Abstract:
Electrophoresis is a widely used analytical technique in the medical and biotechnology industries. It can provide for the determination of thousands of individual compounds on this small scale. The operating conditions are quite conducive to use with the delicate products of genetic engineering. Due to other complexities associated with scale-up, the process is not widely used on a large scale. A novel recycling electrophoretic instrument was investigated as a preparative protein separation device. The process occurs in a thin film of liquid between two flat plates, in a direction perpendicular to the flow. This device was unique in its use of a relatively high flowrate, and recycling of the process fluid as a method for increasing residence time. The apparatus was operated in three modes, isoelectric focusing (IEF), zone electrophoresis (ZE) and isotachophoresis (ITP). For use in the ITP mode, a computer was used for data acquisition and control functions. Model systems included monoclonal antibodies and lentil lectins.
Type:
text; Thesis-Reproduction (electronic)
Keywords:
Isotachophoresis.; Electrophoresis.; Proteins -- Separation -- Technique.
Degree Name:
M.S.
Degree Level:
masters
Degree Program:
Graduate College; Chemical Engineering
Degree Grantor:
University of Arizona
Advisor:
Bier, Milan

Full metadata record

DC FieldValue Language
dc.language.isoen_USen_US
dc.titleRecycling isotachophoresis: A novel approach to preparative protein fractionationen_US
dc.creatorSloan, Jeffrey Edward, 1963-en_US
dc.contributor.authorSloan, Jeffrey Edward, 1963-en_US
dc.date.issued1987en_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.description.abstractElectrophoresis is a widely used analytical technique in the medical and biotechnology industries. It can provide for the determination of thousands of individual compounds on this small scale. The operating conditions are quite conducive to use with the delicate products of genetic engineering. Due to other complexities associated with scale-up, the process is not widely used on a large scale. A novel recycling electrophoretic instrument was investigated as a preparative protein separation device. The process occurs in a thin film of liquid between two flat plates, in a direction perpendicular to the flow. This device was unique in its use of a relatively high flowrate, and recycling of the process fluid as a method for increasing residence time. The apparatus was operated in three modes, isoelectric focusing (IEF), zone electrophoresis (ZE) and isotachophoresis (ITP). For use in the ITP mode, a computer was used for data acquisition and control functions. Model systems included monoclonal antibodies and lentil lectins.en_US
dc.typetexten_US
dc.typeThesis-Reproduction (electronic)en_US
dc.subjectIsotachophoresis.en_US
dc.subjectElectrophoresis.en_US
dc.subjectProteins -- Separation -- Technique.en_US
thesis.degree.nameM.S.en_US
thesis.degree.levelmastersen_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.disciplineChemical Engineeringen_US
thesis.degree.grantorUniversity of Arizonaen_US
dc.contributor.advisorBier, Milanen_US
dc.identifier.proquest1332543en_US
dc.identifier.oclc20021423en_US
dc.identifier.bibrecord.b1838576xen_US
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