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dc.contributor.advisorSammons, David W.en_US
dc.contributor.authorEmmons, Steven Patrick, 1964-
dc.creatorEmmons, Steven Patrick, 1964-en_US
dc.date.accessioned2013-04-03T13:10:03Z
dc.date.available2013-04-03T13:10:03Z
dc.date.issued1991en_US
dc.identifier.urihttp://hdl.handle.net/10150/278022
dc.description.abstractInsulin action has been extensively studied although the exact mechanism by which the binding of this hormone to its receptor causes the observed effects is still obsure. A 90 kd membrane protein may be involved in this mechanism. An attempt was made to purify and make a monoclonal antibody to the 90 kd protein. Several purification methods were attempted and a 2-D electrophoretic procedure developed. Conventional hybridoma production methods were tried as well as a novel hybridoma procedure using selection of J11Dlo cells, culture in LPS/DxSO4, and electrofusion. The resulting monoclonal antibodies to the 90 kd protein were cross-reactive. Furthermore, the immunological results and the presence of the 90 kd protein in several mammalian species suggest that this protein may be evolutionarily conserved and may play a role in insulin action.
dc.language.isoen_USen_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.subjectBiology, Cell.en_US
dc.titleApproaches to purification and generation of monoclonal antibodies of an insulin-sensitive 90 kd proteinen_US
dc.typetexten_US
dc.typeThesis-Reproduction (electronic)en_US
thesis.degree.grantorUniversity of Arizonaen_US
thesis.degree.levelmastersen_US
dc.identifier.proquest1346681en_US
thesis.degree.disciplineGraduate Collegeen_US
thesis.degree.nameM.S.en_US
dc.identifier.bibrecord.b27251524en_US
refterms.dateFOA2018-08-27T12:23:26Z
html.description.abstractInsulin action has been extensively studied although the exact mechanism by which the binding of this hormone to its receptor causes the observed effects is still obsure. A 90 kd membrane protein may be involved in this mechanism. An attempt was made to purify and make a monoclonal antibody to the 90 kd protein. Several purification methods were attempted and a 2-D electrophoretic procedure developed. Conventional hybridoma production methods were tried as well as a novel hybridoma procedure using selection of J11Dlo cells, culture in LPS/DxSO4, and electrofusion. The resulting monoclonal antibodies to the 90 kd protein were cross-reactive. Furthermore, the immunological results and the presence of the 90 kd protein in several mammalian species suggest that this protein may be evolutionarily conserved and may play a role in insulin action.


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