Texas A&M University LibrariesTexas A&M University LibrariesTexas A&M University Libraries
    • Help
    • Login
    OAKTrust
    View Item 
    •   OAKTrust Home
    • Programs, Centers, and Institutes
    • Undergraduate Research and Capstones
    • University Undergraduate Research Fellows (1968–2012)
    • View Item
    •   OAKTrust Home
    • Programs, Centers, and Institutes
    • Undergraduate Research and Capstones
    • University Undergraduate Research Fellows (1968–2012)
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Comparative studies of diverged members of the phosphotriesterase family

    Thumbnail
    View/Open
    2002 Fellows Thesis A762.pdf (2.220Mb)
    Date
    2013-02-22
    Author
    Arriens, Cristina Gale
    Metadata
    Show full item record
    Abstract
    Some genes direct the synthesis of specific proteins called enzymes that catalyze specific types of chemical reactions. The class of enzyme of interest in this research, the hydrolases, catalyzes the conversion of functional groups to water. The phosphotriesterase (PTE) family is a subgroup of hydrolases that breaks down organophosphate compounds (OPs). Many organophosphate compounds are potent cholinesterase inhibitors, accounting for their widespread use as insecticides and nerve agents. Enzymes have been found in bacteria and higher organisms that specifically breakdown OPs. One of these enzymes, human serum paraoxonase/arylesterase (PON1), is a calcium-dependent, HDL (High Density Lipoprotein) -associated protein that appears to have multiple roles in vivo. In one guise, PON1 hydrolyses organophosphate insecticides and nerve gases and is responsible for determining the selective toxicity of these compounds in mammals. Using the sequence available in NCBI Genebank, primers flanking the coding region of PON1 were designed and used to screen a human liver cDNA library using polymerase chain reaction (PCR). A single band corresponding to the approximate size of PON1, 1kb, was amplified and subsequently cloned. The identity of the cloned region as PON1 was verified by sequencing using PON1 specific primers, and then cloned into a plasmid named pTYB1 from the IMPACT-CN expression system. Expression was obtained using the BL21-star bacterial strain. The enzyme was found within an inclusion body, and solubilized with urea and DTT. Preliminary activity studies were unsuccessful, so further manipulation of the insoluble fraction is necessary to obtain proper folding.
    URI
    http://hdl.handle.net/1969.1/ETD-TAMU-2002-Fellows-Thesis-A762
    Description
    Due to the character of the original source materials and the nature of batch digitization, quality control issues may be present in this document. Please report any quality issues you encounter to digital@library.tamu.edu, referencing the URI of the item.
    Includes bibliographical references (leaf 23).
    Subject
    life sciences I.
    Major life sciences I.
    Collections
    • University Undergraduate Research Fellows (1968–2012)
    Citation
    Arriens, Cristina Gale (2002). Comparative studies of diverged members of the phosphotriesterase family. Texas A&M University. Available electronically from http : / /hdl .handle .net /1969 .1 /ETD -TAMU -2002 -Fellows -Thesis -A762.

    DSpace software copyright © 2002-2016  DuraSpace
    Contact Us | Send Feedback
    Theme by 
    Atmire NV
     

     

    Advanced Search

    Browse

    All of OAKTrustCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsDepartmentThis CollectionBy Issue DateAuthorsTitlesSubjectsDepartment

    My Account

    LoginRegister

    Statistics

    View Usage Statistics
    Help and Documentation

    DSpace software copyright © 2002-2016  DuraSpace
    Contact Us | Send Feedback
    Theme by 
    Atmire NV