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Purification and characterization of a carbonyl-reductase from human liver, which is competent in the reduction of 6-pyruvoyl-tetrahydropterin

Purification and characterization of a carbonyl-reductase from human liver, which is competent in the reduction of 6-pyruvoyl-tetrahydropterin

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STEINERSTAUCH, Petra, Yoshitomo SAWADA, Walter LEIMBACHER, Sandro GHISLA, Hans-Christoph CURTIUS, 1989. Purification and characterization of a carbonyl-reductase from human liver, which is competent in the reduction of 6-pyruvoyl-tetrahydropterin. In: Pteridines. 1(4), pp. 189-198. ISSN 0933-4807. eISSN 2195-4720

@article{Steinerstauch1989Purif-8583, title={Purification and characterization of a carbonyl-reductase from human liver, which is competent in the reduction of 6-pyruvoyl-tetrahydropterin}, year={1989}, doi={10.1515/pteridines.1989.1.4.189}, number={4}, volume={1}, issn={0933-4807}, journal={Pteridines}, pages={189--198}, author={Steinerstauch, Petra and Sawada, Yoshitomo and Leimbacher, Walter and Ghisla, Sandro and Curtius, Hans-Christoph} }

<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/123456789/8583"> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:44:52Z</dc:date> <dcterms:issued>1989</dcterms:issued> <dc:contributor>Leimbacher, Walter</dc:contributor> <dcterms:abstract xml:lang="eng">An enzyme which reduces 6-pyruvoyl-tetrahydropterin has been purified to apparent homogeneity from human liver. It consists of a single polypeptide chain with a molecular weight of 35 kDa, has an isoelectric point of 5.9 ± 0.1 and contains no glycosyl residues. The pure enzyme has a specific activity of 450 mU/mg protein at pH 7.0 in 10 mM potassium phosphate buffer. It converts 6-pyruvoyl-tetrahydropterin to 6-lactoyltetrahydropterin by transfer of the pro 4R-hydrogen of NADPH to form the side chain -OH at position C(2') of the substrate. Km values are 1.8 μM for 6-pyruvoyl-tetrahydropterin and 5.5 μM for NADPH. Polyclonal antibodies raised against the purified enzyme recognize 6-pyruvoyl-tetrahydropterin reductase in Western blot and ELISA but do not cross-react with human sepiapterin reductase. The enzyme appears to be identical with aldose reductase.</dcterms:abstract> <dc:creator>Curtius, Hans-Christoph</dc:creator> <dc:contributor>Curtius, Hans-Christoph</dc:contributor> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8583"/> <dc:format>application/pdf</dc:format> <dc:creator>Ghisla, Sandro</dc:creator> <dc:contributor>Sawada, Yoshitomo</dc:contributor> <dcterms:bibliographicCitation>First publ. in: Pteridines 1 (1989), 4, pp. 189-198</dcterms:bibliographicCitation> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:44:52Z</dcterms:available> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:creator>Sawada, Yoshitomo</dc:creator> <dc:contributor>Ghisla, Sandro</dc:contributor> <dc:creator>Leimbacher, Walter</dc:creator> <dc:rights>deposit-license</dc:rights> <dc:creator>Steinerstauch, Petra</dc:creator> <dcterms:title>Purification and characterization of a carbonyl-reductase from human liver, which is competent in the reduction of 6-pyruvoyl-tetrahydropterin</dcterms:title> <dc:contributor>Steinerstauch, Petra</dc:contributor> <dc:language>eng</dc:language> </rdf:Description> </rdf:RDF>

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