Date of Award
5-2006
Degree Type
Thesis
Degree Name
Departmental Honors
Department
Chemistry and Biochemistry
Abstract
A strain of Escherichia coli was genetically modified to co-express human heme oxygenase-1 and ferritin. The E. coli were then grown with varying amounts of hemin to see if the iron released upon degradation of the hemin by heme oxygenase-1 is loaded into ferritin. Following incubation, the ferritin was purified and the amount of iron loaded into ferritin determined. It was found that ferritin purifed from E. coli expressing human heme oxygenase-1 contained more iron than E. coli that did not contain human heme oxygenase-1. It was concluded that some of the iron released upon degradation of hemin by heme oxygenase-1 can be sequestered by ferritin.
Recommended Citation
Gardner, Jonathan Mark, "The Fate of Iron Released from Heme by Hemeoxygenase-1" (2006). Undergraduate Honors Capstone Projects. 753.
https://digitalcommons.usu.edu/honors/753
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Faculty Mentor
Steven D. Aust
Departmental Honors Advisor
Steve Scheiner