Publikation: Prostaglandin 9-ketoreductase from pig and human kidney : purification, properties and identity with human carbonyl reductase
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1992
Autor:innen
Schieber, Ardrea
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Eicosanoids. 1992, 5(Suppl), pp. 37-38
Zusammenfassung
Prostaglandin 9-ketoreductase has been purified to apparent homogeneity from pig and human kidney with an overall yield of 6%. The enzyme has a molecular mass of 34 kDa, it is present as an active monomer in diluted solution and contains approx. 2 equivalents Zn++/mole enzyme. It is stereoselective for the pro(S) hydrogen of NADPH and reduces the prostaglandin 9-keto group to yield 90% prostaglandin F2α and 8% of the ß-form. An extensive study of the catalytic properties was carried out, which leads ta the conclusion that the enzyme function in vivo is unlikely a catalysis of oxidation/reduction at the prostaglandin 9-position. Five peptides from the pig kidney enzyme were sequenced and compared with the sequence of carbonyl reductase from human placenta. The identity is > 90% and this, together with the immunological cross-reactivity with human brain carbonyl reductase, most strongly suggests that prostaglandin 9-ketoreductase and carbonyl reductase are the same enzyme.
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Fachgebiet (DDC)
570 Biowissenschaften, Biologie
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Prostaglandin-9-ketoreductase, human carbonyl reductase, purification, mechanism, specificity, amino acid sequence, physiological function
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SCHIEBER, Ardrea, Sandro GHISLA, 1992. Prostaglandin 9-ketoreductase from pig and human kidney : purification, properties and identity with human carbonyl reductase. In: Eicosanoids. 1992, 5(Suppl), pp. 37-38BibTex
@article{Schieber1992Prost-8591,
year={1992},
title={Prostaglandin 9-ketoreductase from pig and human kidney : purification, properties and identity with human carbonyl reductase},
number={Suppl},
volume={5},
journal={Eicosanoids},
pages={37--38},
author={Schieber, Ardrea and Ghisla, Sandro}
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<dcterms:abstract xml:lang="eng">Prostaglandin 9-ketoreductase has been purified to apparent homogeneity from pig and human kidney with an overall yield of 6%. The enzyme has a molecular mass of 34 kDa, it is present as an active monomer in diluted solution and contains approx. 2 equivalents Zn++/mole enzyme. It is stereoselective for the pro(S) hydrogen of NADPH and reduces the prostaglandin 9-keto group to yield 90% prostaglandin F2α and 8% of the ß-form. An extensive study of the catalytic properties was carried out, which leads ta the conclusion that the enzyme function in vivo is unlikely a catalysis of oxidation/reduction at the prostaglandin 9-position. Five peptides from the pig kidney enzyme were sequenced and compared with the sequence of carbonyl reductase from human placenta. The identity is > 90% and this, together with the immunological cross-reactivity with human brain carbonyl reductase, most strongly suggests that prostaglandin 9-ketoreductase and carbonyl reductase are the same enzyme.</dcterms:abstract>
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