• Login
    View Item 
    •   Home
    • Massey Documents by Type
    • Theses and Dissertations
    • View Item
    •   Home
    • Massey Documents by Type
    • Theses and Dissertations
    • View Item
    JavaScript is disabled for your browser. Some features of this site may not work without it.

    Purification and properties of uracil dehydrogenase from Nocardia corallina :|ba thesis presented in partial fulfilment of the requirements for the degree of Doctor of Philosophy in Biochemistry at Massey University, New Zealand

    Icon
    View/Open Full Text
    02_whole.pdf (9.045Mb)
    01_front.pdf (1.456Mb)
    Export to EndNote
    Abstract
    Uracil dehydrogenase (EC 1.2.99.1), an enzyme which catalysed the oxidation of uracil or thymine to the corresponding barbituric acids, has been purified in a typical preparation, 85-fold with an 18% recovery of the initial activity present in a cell-free extract from Nocardia corallina. The enzyme was considered to be 95-98% pure by gel electrophoresis. It has a molecular weight of approximately 298 000, determined by both gel filtration and sedimentation equilibrium centrifugation and consists of two each of three dissimilar subunits, with molecular weights of 91 000, 36 000 and 21 000 as determined by sodium dodecyl sulphate - polyacrylamide gel electrophoresis. The spectrum of the enzyme is similar to that of milk xanthine oxidase and rabbit liver aldehyde oxidase (Rajagopalan & Handler, 1964), and is typical of nonheme iron flavoproteins. The flavin prosthetic group was identified as flavin adenine dinucleotide. It was demonstrated that the enzyme contains, per mole of protein, 1 mole of FAD, 4 atoms of nonheme iron and 4 moles of labile sulphide. The amino acid composition of uracil dehydrogenase has been determined. Other properties reported for the enzyme include substrate and electron acceptor specificity, Km for uracil and thymine, pH optimum, and the effect of various inhibitors on enzyme activity. In addition, the purified enzyme has been shown to exhibit 'aerobic dehydrogenase' activity.
    Date
    1976
    Author
    Payakachat, Taypin
    Rights
    The Author
    Publisher
    Massey University
    URI
    http://hdl.handle.net/10179/3781
    Collections
    • Theses and Dissertations
    Metadata
    Show full item record

    Copyright © Massey University
    | Contact Us | Feedback | Copyright Take Down Request | Massey University Privacy Statement
    DSpace software copyright © Duraspace
    v5.7-2020.1-beta1
     

     

    Tweets by @Massey_Research
    Information PagesContent PolicyDepositing content to MROCopyright and Access InformationDeposit LicenseDeposit License SummaryTheses FAQFile FormatsDoctoral Thesis Deposit

    Browse

    All of MROCommunities & CollectionsBy Issue DateAuthorsTitlesSubjectsThis CollectionBy Issue DateAuthorsTitlesSubjects

    My Account

    LoginRegister

    Statistics

    View Usage Statistics

    Copyright © Massey University
    | Contact Us | Feedback | Copyright Take Down Request | Massey University Privacy Statement
    DSpace software copyright © Duraspace
    v5.7-2020.1-beta1