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    The Development of a Quantitative Assay to Measure the Effects of Protein Disulfide Isomerase on Prion Protein Misfolding

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    2010_VoglL_THS_000553.pdf (5.991Mb)
    Author
    Vogl, Lauren
    Date of Issue
    2010-04-01
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    URI
    https://scholars.carroll.edu/handle/20.500.12647/2850
    Title
    The Development of a Quantitative Assay to Measure the Effects of Protein Disulfide Isomerase on Prion Protein Misfolding
    Type
    thesis
    Abstract
    The objective ofthis project was to develop a quantitative assay to measure the misfolding ofprion proteins that can be used to assess the effects of Protein Disulfide Isomerase (PDI) on the misfolding process ofthe Chronic Wasting Disease (CWD) prion protein. CWD is a spongiform encephalopathy native to animals in the family Cervidae, which includes whitetail deer, mule deer, elk and moose. CWD is caused by the misfolding ofprion proteins. Qualitative observations from previous studies indicate that disulfide bond rearrangement might be a rate limiting step in the misfolding process. There is a need to be able to quantitate the amount of misfolded prion protein, and this was achieved through a limiting dilution, slot blot analysis using a Bio Dot® SF Microfiltration apparatus. The limiting dilution, slot blot analysis was standardized parallel with conventional immunoblotting and was optimized using differing buffers and immunoblot membranes. This quantitative technique can be used to measure the effect of PDI on the misfolding of CWD prion proteins.
    Degree Awarded
    Bachelor's
    Semester
    Spring
    Department
    Life & Environmental Sciences
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    • Life and Environmental Sciences Undergraduate Theses

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