Partial purification of human placental 15-hydroxyprostaglandin dehydrogenase: Kinetic properties

W. Schlegel, Laurence M. Demers, Helga E. Hilldebrandt-Stark, Harold R. Behrman, Roy O. Greep

Research output: Contribution to journalArticlepeer-review

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The enzyme system, 15-hydroxyprostaglandin dehydrogenase, which catalyzes the first inactivation step in the catabolism of the prostaglandins has been isolated and purified 107-fold from human placenta. Kinetic studies reveal different Michaelis-Menten constants for most of the naturally occurring prostaglandins. The Km for PGE2 was found to be 10 μM, for PGE1, 27 μM; for PGA2, 32 μM; for PGA1, 33 μM; and for PGF 59 μM. The enzyme has a sharp pH-optimum between 7.5 and 8.8. Prostaglandin dehydrogenase appears to be isoenzymic as judged by separation on polyacrylamide disc gel electrophoresis. Inhibition studies with the partially purified enzyme indicate that progesterone and estrogen may influence the conversion of biologically active prostaglandins into the biologically inactive 15-ketoprostaglandins. These findings offer evidence for the control of prostaglandin metabolism in the human placenta.

Original languageEnglish (US)
Pages (from-to)417-433
Number of pages17
Issue number5
StatePublished - Mar 10 1974

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Endocrinology


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