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Purification and properties of prostaglandin 9-ketoreductase from pig and human kidney : identity with human carbonyl reductase

Purification and properties of prostaglandin 9-ketoreductase from pig and human kidney : identity with human carbonyl reductase

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SCHIEBER, Ardrea, Rainer W. FRANK, Sandro GHISLA, 1992. Purification and properties of prostaglandin 9-ketoreductase from pig and human kidney : identity with human carbonyl reductase. In: European Journal of Biochemistry. 206(2), pp. 491-502. eISSN 0014-2956. Available under: doi: 10.1111/j.1432-1033.1992.tb16952.x

@article{Schieber1992Purif-6550, title={Purification and properties of prostaglandin 9-ketoreductase from pig and human kidney : identity with human carbonyl reductase}, year={1992}, doi={10.1111/j.1432-1033.1992.tb16952.x}, number={2}, volume={206}, journal={European Journal of Biochemistry}, pages={491--502}, author={Schieber, Ardrea and Frank, Rainer W. and Ghisla, Sandro} }

Frank, Rainer W. eng application/pdf Schieber, Ardrea Purification and properties of prostaglandin 9-ketoreductase from pig and human kidney : identity with human carbonyl reductase Ghisla, Sandro 2011-03-24T17:27:20Z Ghisla, Sandro 2011-03-24T17:27:20Z 1992 Frank, Rainer W. Prostaglandin 9-ketoreductase (PG-9-KR) was purified from pig kidney to homogeneity, as judged by SDS/PAGE using an improved procedure. The enzyme is pro-S stereoselective with regard to hydrogen transfer from NADPH with prostaglandin E2 as substrate and reduces its 9-keto group with approximately 90% stereoselectivity to form prostaglandin F2α. Approximately 8% of the prostaglandin F formed has the β-configuration. In addition to catalyzing the interconversion of prostaglandin E2 to F2α, PG-9-KR also oxidizes prostaglandin E2, F2α and D2 to their corresponding, biologically inactive, 15-keto metabolites. Incubation of PG-9-KR with prostaglandin F2α and NAD+ leads to the preferential formation of 15-keto prostaglandin F2α rather than prostaglandin E2. This suggests that the prostaglandin E2/prostaglandin F2α ratio is not determined by the NADP+/NADPH redox couple. The enzyme also reduces various other carbonyl compounds (e.g. 9,10-phen-anthrenequinone) with high efficiency. The catalytic properties measured for PG-9-KR suggest that its in vivo function is unlikely to be to catalyze formation of prostaglandin F2α. The monomeric enzyme has a molecular mass of 32 kDa and exists as four isoforms, as judged by isoelectric focusing. PG-9-KR contains 1.9 mol Zn2+/mol enzyme and no other cofactors. Human kidney PG-9-KR was also purified to homogeneity. The human enzyme has a molecular mass of 34 kDa and also exists as four isoforms. Polyclonal antibodies raised against pig kidney PG-9-KR cross-react with human kidney PG-9-KR and also with human brain carbonyl reductase, as demonstrated by Western blot analysis. Sequence data of tryptic peptides from pig kidney PG-9-KR show >90% identity with human placenta carbonyl reductase. From comparison of several properties (catalytical, structural and immunological properties), it is concluded that PG-9-KR and carbonyl reductase are identical enzymes. deposit-license Schieber, Ardrea First publ. in: European Journal of Biochemistry 206 (1992), 2, pp. 491-502

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