Purification of the Bovine Xanthine Oxidoreductase from Milk Fat Globule Membranes and Cloning of Complementary Deoxyribonucleic Acid

L. Berglund*, J. T. Rasmussen, M. D. Andersen, M. S. Rasmussen, T. E. Petersen

*Corresponding author af dette arbejde

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    Abstract

    The amino acid sequence of the bovine xanthine oxidoreductase was determined by cloning and sequencing cDNA clones encoding the enzyme. Partial amino acid sequences corresponding to 54% of the total sequence were also determined from purified bovine milk xanthine oxidoreductase, showing identity with the translated cDNA sequence. The cDNA of 4719 nucleotides included a 5′ untranslated region of 96 nucleotides, an open reading frame encoding a xanthine oxidoreductase of 1332 amino acid residues, and a 3′ untranslated region of 624 nucleotides including two polyadenylation signals and a poly(A) tail of 74 nucleotides. The identity between the amino acid sequence of the bovine xanthine oxidoreductase and xanthine oxidoreductase from mammalian species was 86 to 90%.

    OriginalsprogEngelsk
    TidsskriftJournal of Dairy Science
    Vol/bind79
    Nummer2
    Sider (fra-til)198-204
    Antal sider7
    ISSN0022-0302
    DOI
    StatusUdgivet - 1996

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