@article{Takikawa1986Purif-8308,
  year={1986},
  doi={10.1016/S0006-291X(86)80468-5},
  title={Purification of 6-pyruvoyl-tetrahydropterin synthase from human liver},
  number={2},
  volume={134},
  issn={0006-291X},
  journal={Biochemical and Biophysical Research Communications},
  pages={646--651},
  author={Takikawa, Shin-Ichiro and Curtius, Hans-Christoph and Redweik, Udo and Ghisla, Sandro}
}

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    <dc:contributor>Ghisla, Sandro</dc:contributor>
    <dc:creator>Curtius, Hans-Christoph</dc:creator>
    <dcterms:title>Purification of 6-pyruvoyl-tetrahydropterin synthase from human liver</dcterms:title>
    <dc:creator>Redweik, Udo</dc:creator>
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    <dc:rights>Attribution-NonCommercial-NoDerivs 2.0 Generic</dc:rights>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:42:34Z</dc:date>
    <dc:creator>Takikawa, Shin-Ichiro</dc:creator>
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    <dc:contributor>Redweik, Udo</dc:contributor>
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    <dcterms:abstract xml:lang="eng">The enzyme which catalyzes the first step in the conversion of dihydroneopterin triphosphate to tetrahydrobiopterin has been purified approx. 40,000-fold from human liver to apparent homogeneity. The enzyme has a native molecular weight of ~83,000 and consists of four identical subunits, each of which has a molecular weight of ~19,000. It contains carbohydrates and is remarkably stable to heat treatment. In the presence of purified sepiapterin reductase, Mg2+, and NADPH, this enzyme catalyzes efficiently the formation of tetrahydrobiopterin from dihydroneopterin triphosphate. This indicates that these two proteins are sufficient for the overall conversion.</dcterms:abstract>
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    <dc:contributor>Curtius, Hans-Christoph</dc:contributor>
    <dcterms:bibliographicCitation>First publ. in: Biochemical and Biophysical Research Communications 134 (1986), 2, pp. 646-651</dcterms:bibliographicCitation>
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