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

doi:10.1016/S0090-6980(74)80011-0

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

Department of Pathology and Laboratory Medicine

Research output: Contribution to journal › Article › peer-review

59 Scopus citations

Abstract

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 K_m for PGE₂ was found to be 10 μM, for PGE₁, 27 μM; for PGA₂, 32 μM; for PGA₁, 33 μM; and for PGF_2α 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 language	English (US)
Pages (from-to)	417-433
Number of pages	17
Journal	Prostaglandins
Volume	5
Issue number	5
DOIs	https://doi.org/10.1016/S0090-6980(74)80011-0
State	Published - Mar 10 1974

All Science Journal Classification (ASJC) codes

Biochemistry
Endocrinology

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10.1016/S0090-6980(74)80011-0

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@article{883da126268145748a21f18d60f0e6e0,

title = "Partial purification of human placental 15-hydroxyprostaglandin dehydrogenase: Kinetic properties",

abstract = "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 PGF2α 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.",

author = "W. Schlegel and Demers, {Laurence M.} and Hilldebrandt-Stark, {Helga E.} and Behrman, {Harold R.} and Greep, {Roy O.}",

note = "Funding Information: Supported by NIH Grant HD-O3736, The Ford Foundation, Merck Sharp and Dohme and by a Fellowship from Deutsche Forschungsgemelnschaft Schl. 140/2. We thank Dr. John R. Paulsrud, Hoffman-La Roche, Inc., N.J. for recording the substrate dependency of the enzyme and Anne Ehrlich for her skillful technical assistance.",

year = "1974",

month = mar,

day = "10",

doi = "10.1016/S0090-6980(74)80011-0",

language = "English (US)",

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pages = "417--433",

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T1 - Partial purification of human placental 15-hydroxyprostaglandin dehydrogenase

T2 - Kinetic properties

AU - Schlegel, W.

AU - Demers, Laurence M.

AU - Hilldebrandt-Stark, Helga E.

AU - Behrman, Harold R.

AU - Greep, Roy O.

N1 - Funding Information: Supported by NIH Grant HD-O3736, The Ford Foundation, Merck Sharp and Dohme and by a Fellowship from Deutsche Forschungsgemelnschaft Schl. 140/2. We thank Dr. John R. Paulsrud, Hoffman-La Roche, Inc., N.J. for recording the substrate dependency of the enzyme and Anne Ehrlich for her skillful technical assistance.

PY - 1974/3/10

Y1 - 1974/3/10

N2 - 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 PGF2α 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.

AB - 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 PGF2α 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.

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ER -

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

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