Publikation: Purification and characterization of a carbonyl-reductase from human liver, which is competent in the reduction of 6-pyruvoyl-tetrahydropterin
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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.
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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. 1989, 1(4), pp. 189-198. ISSN 0933-4807. eISSN 2195-4720. Available under: doi: 10.1515/pteridines.1989.1.4.189BibTex
@article{Steinerstauch1989Purif-8583, year={1989}, doi={10.1515/pteridines.1989.1.4.189}, title={Purification and characterization of a carbonyl-reductase from human liver, which is competent in the reduction of 6-pyruvoyl-tetrahydropterin}, 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} }
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