Insulin 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.
Identifer | oai:union.ndltd.org:arizona.edu/oai:arizona.openrepository.com:10150/278022 |
Date | January 1991 |
Creators | Emmons, Steven Patrick, 1964- |
Contributors | Sammons, David W. |
Publisher | The University of Arizona. |
Source Sets | University of Arizona |
Language | en_US |
Detected Language | English |
Type | text, Thesis-Reproduction (electronic) |
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. |
Page generated in 0.0086 seconds