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Simplified Purification of GST-tagged Proteins

Undergraduate #146
Discipline: Chemistry and Chemical Sciences
Subcategory: Biochemistry (not Cell and Molecular Biology and Genetics)

Susan Campbell - Louisiana Tech University
Co-Author(s): Mercede Furr and Thallapuranam Krishnaswamy Suresh Kumar, University of Arkansas, Fayetteville, AR



The purification of proteins for use in research and medical fields is a costly and time consuming procedure when using the current methods available. This research formulates a new purification method for GST-tagged proteins. The fusion protein of GST-cpSRP43 was first overexpressed in E. coli. This protein was then successfully purified following cleavage through the use of heat treatment in order to precipitate the GST-affinity tag. The results of this research are anticipated to make the purification of GST-tagged proteins that are heat stable a much easier and more cost friendly procedure.

Funder Acknowledgement(s): NSF grant CHE-1263119/REU, NIH grant (P30 GM 103450), NSF grant IOS-0842937, DOE grant DE-02-01ER15161.

Faculty Advisor: Thallapuranam Krishnaswamy Suresh Kumar, sthalla@uark.edu

Role: I lysed the cells and separated the components using centrifugation. I verified the purification of the the affinity protein using a GSH-Sepharose column. I then performed multiple heat treatments and cleavage experiments on the proteins and ran SDS-PAGE gels in order to monitor the results of the results of the experiments.

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This material is based upon work supported by the National Science Foundation (NSF) under Grant No. DUE-1930047. Any opinions, findings, interpretations, conclusions or recommendations expressed in this material are those of its authors and do not represent the views of the AAAS Board of Directors, the Council of AAAS, AAAS’ membership or the National Science Foundation.

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