首頁 > 網路資源 > 大同大學數位論文系統

Title page for etd-0721109-155941


URN etd-0721109-155941 Statistics This thesis had been viewed 3185 times. Download 1854 times.
Author Yi-chen Chen
Author's Email Address No Public.
Department Bioengineering
Year 2008 Semester 2
Degree Master Type of Document Master's Thesis
Language zh-TW.Big5 Chinese Page Count 153
Title Preparation of high affinity molecularly imprinted
polymers selective for denatured creatine kinase and
their application to the extraction of native and
denatured proteins
Keyword
  • creatine kinase
  • denatured protein
  • molecularly imprinted polymer
  • sodium dodecyl sulfate
  • sodium dodecyl sulfate
  • molecularly imprinted polymer
  • denatured protein
  • creatine kinase
  • Abstract The inter-relationship of protein structure and function is of interest to
    many researchers; however, formal academic study of denatured proteins,
    arising e.g. from genetic mutations, has until now been limited. Of critical
    significance are the degenerative processes that lead to the conversion of the
    α-helix to the β-sheet, and the generation of amyloid plaques in for example:
    Alzheimer’s disease, Parkinson’s disease and degenerative conditions
    associated with prions.
    Here a simple synthetic approach based on micro- contact imprinting
    has been used to form imprints of the secondary structure of creatine kinase
    (CK), denatured by treatment with SDS. The imprinted materials, formed with MMA and PEG400DMA, in a volume ratio of 5:95, have been
    demonstrated to be able to separate denatured CK from its native from.
    Using NaOH/trypsin, a template extraction-efficiency, i.e. denatured CK
    removal from the film, of 90% was obtained. Subsequent re-binding of the
    template, i.e. denatured CK, was typically 70%, (template solution 3.5 ×10 -7
    mol, MIP surface area 1.69 cm2), with an imprinting efficiency of 9.7.
    Evaluation of the imprinted polymers in non-competitive re-binding
    experiments with native and denatured proteins, showed re-binding of 68.3%,
    95.3%, 92.3% and 62.4% to the native forms of CK, IgG, HSA and myoglobin respectively; while the respective binding to denatured forms of
    IgG, HSA and myoglobin was 94.1%, 92.7%, 71.7%. In a competitive binary
    system, using the denatured forms of: IgG, HSA and myoglobin; the
    selectivity was 98.7%, 96.8% and 63.8%, respectively.
    The method used has been shown to be a successful approach for the
    formation of high-affinity materials able to separate denatured CK from its
    native form and from other denatured proteins. Such materials may find
    future applications in practical sensing devices.
    Advisor Committee
  • Chung-yih Wang - advisor
  • Tse-chuan Chou - advisor
  • Kuo-chuan Ho - co-chair
  • Files indicate access worldwide
    Date of Defense 2009-06-26 Date of Submission 2009-07-21


    Browse | Search All Available ETDs