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

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avis › Tidsskriftartikel › Forskning › peer review

DOI

  • L. Berglund, Protein Chemistry Laboratory
    • ,
  • J. T. Rasmussen
  • M. D. Andersen, Protein Chemistry Laboratory, Aarhus Universitet
    • ,
  • M. S. Rasmussen, Protein Chemistry Laboratory
    • ,
  • T. E. Petersen, Protein Chemistry Laboratory

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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