Date Thesis Awarded

6-2010

Access Type

Honors Thesis -- Access Restricted On-Campus Only

Degree Name

Bachelors of Science (BS)

Department

Chemistry

Advisor

Lisa M. Landino

Committee Members

Christopher J. Abelt

Margaret Somosi Saha

Carey Bagdassarian

Abstract

The effects of oxidative damage and the mechanisms through which it is repaired have been a topic of intense research for several years. Research has shown that small changes in the redox state of cells can lead to protein modification which, in turn, can result in changes in protein function and activity. This thesis discusses the development of a method to study tubulin S-glutathionylation that avoids several of the inherent technical difficulties in studying oxidative modifications of tubulin. Biotinylated GSSG (oxidized glutathione) was synthesized, purified, and incorporated into tubulin via thiol-disulfide exchange. S-glutathionylated tubulin was isolated on an avidin-agarose resin by utilization of biotin's affinity for avidin. This biotin affinity capture method allows for future quantification of S-glutathionylation in tubulin as well as exploration of its role in polymerization regulation.

Creative Commons License

Creative Commons License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.

Comments

Thesis is part of Honors ETD pilot project, 2008-2013. Migrated from Dspace in 2016.

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