Perpetua: The UAH Journal of Undergraduate Research


College of Science


Biological Sciences


Protein purification requires an intensive multi-step process that is customized to every protein’s characteristic for optimal results. In this study, we looked at the purification process of Inorganic Pyrophosphatase (IPPase), an essential protein found in all living organisms. The commonality of the protein does not veil the fact that the mechanism by which IPPase is hydrolyzed into two orthophosphates is not fully understood. To comprehend the mechanism, recombinant mutants of the conservative region in IPPase were expressed. However, to observe a possible change in structure of the recombinant mutants with crystallization, pure concentrated protein is needed. Therefore, protein purification is crucial. During this purification process, three characteristics of IPPase are manipulated to create an acceptable purification: IPPase’s thermophilic nature, its isoelectric point, and the 21 kDa size of the monomer. With the perfection of functioning protocol, steps can begin to be taken in the studying of the activity of each integral amino acid.



To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.