Prostaglandin-E2 9-reductase from corpus luteum of pseudopregnant rabbit is a member of the aldo-keto reductase superfamily featuring 20 alpha-hydroxysteroid dehydrogenase activity.
作者： Norbert Wintergalen , Hubert Heinrich Thole , Hans-Joachim Galla , Werner Schlegel
DOI: 10.1111/J.1432-1033.1995.264_C.X
关键词: Enzyme 、 Corpus luteum 、 Non-competitive inhibition 、 Reductase 、 Aldo-keto reductase 、 Biochemistry 、 20-alpha-Hydroxysteroid Dehydrogenase 、 Biology 、 Dehydrogenase 、 Luteolysis
摘要: The prostaglandin-E2 9-reductase (PGE2 9-reductase) activity in the corpus luteum of rabbits corresponds to a cytosolic, NADPH-dependent enzyme with molecular mass 36 kDa. This was purified from corpora lutea on day 12 pseudopregnancy 266-fold enrichment. main purification step affinity chromatography using Red Sepharose CL-6B. efficiency this column improved by elution 1 mM NADH prior active fractions NADPH. Amino acid sequence data demonstrate that rabbit luteal PGE2 has be classified as member aldo-keto reductase superfamily. revealed wide substrate specificity comprising reduction aldehydes, ketones, and quinones. Apparent kinetic constants were determined methylglyoxal, DL-glyceraldehyde, 9,10-phenanthrenquinone substrates. fully showed two catalytic activities particular interest: 20α-hydroxysteroid dehydrogenase (20α-HSD) activities. competitive inhibition 20α-HSD indicates progesterone are substrates for same enzyme. From these results, we conclude prostaglandin steroid metabolism tightly linked each other. For reason could key cascade events leading regression rabbit.
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