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J Dairy Sci. 1996 Feb;79(2):198-204.

Purification of the bovine xanthine oxidoreductase from milk fat globule membranes and cloning of complementary deoxyribonucleic acid.

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1
Protein Chemistry Laboratory, University of Aarhus, Denmark.

Abstract

The amino acid sequence of the bovine xanthine oxidoreductase was determined by cloning and sequencing cDNA clones encoding the enzyme. Partial amino acid sequence 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%.

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