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Purification of 6-pyruvoyl-tetrahydropterin synthase from human liver

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1986

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Takikawa, Shin-Ichiro
Curtius, Hans-Christoph
Redweik, Udo

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Biochemical and Biophysical Research Communications. 1986, 134(2), pp. 646-651. ISSN 0006-291X. Available under: doi: 10.1016/S0006-291X(86)80468-5

Zusammenfassung

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.

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570 Biowissenschaften, Biologie

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ISO 690TAKIKAWA, Shin-Ichiro, Hans-Christoph CURTIUS, Udo REDWEIK, Sandro GHISLA, 1986. Purification of 6-pyruvoyl-tetrahydropterin synthase from human liver. In: Biochemical and Biophysical Research Communications. 1986, 134(2), pp. 646-651. ISSN 0006-291X. Available under: doi: 10.1016/S0006-291X(86)80468-5
BibTex
@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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