Purification of 6-pyruvoyl-tetrahydropterin synthase from human liver

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TAKIKAWA, 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. 134(2), pp. 646-651. ISSN 0006-291X

@article{Takikawa1986Purif-8308, title={Purification of 6-pyruvoyl-tetrahydropterin synthase from human liver}, year={1986}, doi={10.1016/S0006-291X(86)80468-5}, 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} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/8308"> <dc:creator>Takikawa, Shin-Ichiro</dc:creator> <dc:contributor>Curtius, Hans-Christoph</dc:contributor> <dc:creator>Redweik, Udo</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:42:34Z</dcterms:available> <dcterms:title>Purification of 6-pyruvoyl-tetrahydropterin synthase from human liver</dcterms:title> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:contributor>Redweik, Udo</dc:contributor> <dc:contributor>Takikawa, Shin-Ichiro</dc:contributor> <dcterms:bibliographicCitation>First publ. in: Biochemical and Biophysical Research Communications 134 (1986), 2, pp. 646-651</dcterms:bibliographicCitation> <dc:rights>deposit-license</dc:rights> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8308"/> <dc:contributor>Ghisla, Sandro</dc:contributor> <dc:creator>Curtius, Hans-Christoph</dc:creator> <dcterms:issued>1986</dcterms:issued> <dc:language>eng</dc:language> <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> <dc:creator>Ghisla, Sandro</dc:creator> <dc:format>application/pdf</dc:format> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:42:34Z</dc:date> </rdf:Description> </rdf:RDF>

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