• Login
    View Item 
    •   Carroll Scholars Home
    • Life and Environmental Sciences
    • Life and Environmental Sciences Undergraduate Theses
    • View Item
    •   Carroll Scholars Home
    • Life and Environmental Sciences
    • Life and Environmental Sciences Undergraduate Theses
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    The Effect of Protein Disulfide Isomerase (PDI) on In Vitro Conversion of Mule Deer Prion Proteins

    Thumbnail
    View/Open
    2009_NixonA_THS_000600.pdf (5.606Mb)
    Author
    Nixon, Alexander
    Date of Issue
    2009-04-01
    Subject Keywords
    prion, disease, Chronic Wasting Disease
    Metadata
    Show full item record
    URI
    https://scholars.carroll.edu/handle/20.500.12647/2867
    Title
    The Effect of Protein Disulfide Isomerase (PDI) on In Vitro Conversion of Mule Deer Prion Proteins
    Type
    thesis
    Abstract
    The objective of this project was to study Chronic Wasting Disease (CWD), a form of spongiform encephalopathy native to animals in the family Cervidae. The infectious agent in CWD is a misfolded form of the prion protein (PrPSc), which has undergone conversion from the normal, cellular prion protein (PrPc). The prion protein contains a disulfide bond, and the current project examined whether disulfide bond rearrangement is involved in the misfolding process. Using Protein Disulfide Isomerase (PDI), an enzyme that accelerates disulfide rearrangement, the efficiency of prion protein misfolding was monitored. Two different sources of normal prion protein were used: deer brain (dPrPc) and recombinant (rPrPc). Two different in vitro misfolding assays were also used in the study. Initial results suggest that prion misfolding was enhanced in the presence of PDI. This indicates that disulfide bond rearrangement may occur during the conversion of normal prion protein to the misfolded, disease causing form. Furthermore, this study indicates that in vitro conversion analysis may be an effective approach to monitoring prion conversion dynamics. Further work will enable this approach to be used to quantitatively evaluate prion misfolding kinetics.
    Degree Awarded
    Bachelor's
    Semester
    Spring
    Department
    Life & Environmental Sciences
    Collections
    • Life and Environmental Sciences Undergraduate Theses

    Browse

    All of Carroll ScholarsCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

    My Account

    LoginRegister

    DSpace software copyright © 2002-2023  DuraSpace
    DSpace Express is a service operated by 
    Atmire NV