| Kinetic studies on 15-hydroxyprostaglandin dehydrogenase from human placenta. | |
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MedLine Citation:
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PMID: 187034 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The enzyme system 15-hydroxyprostaglandin dehydrogenase, which catalyzes the oxidation of the 15-hydroxy group of all naturally occurring prostaglandins, has been purified 1,270-fold by isoelectric focusing. Km values have been determined for prostaglandin E2 and NAD+ and were found to be 1 and 44 muM. The overall forward reaction was V1 = 450 nmol/min. Both the product 15-ketoprostaglandin E2 and the metabolite 13,14-dihydro-15-ketoprostaglandin E2 were noncompetitive inhibitors for the enzyme. |
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Authors:
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W Schlegel; R O Greep |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Advances in prostaglandin and thromboxane research Volume: 1 ISSN: 0361-5952 ISO Abbreviation: Adv Prostaglandin Thromboxane Res Publication Date: 1976 |
Date Detail:
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Created Date: 1977-01-25 Completed Date: 1977-01-25 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 7610366 Medline TA: Adv Prostaglandin Thromboxane Res Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 159-62 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Alcohol Oxidoreductases
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metabolism* Female Humans Hydroxyprostaglandin Dehydrogenases / antagonists & inhibitors, isolation & purification, metabolism* Kinetics NAD / metabolism Placenta / enzymology* Pregnancy Prostaglandins E / metabolism |
| Chemical | |
Reg. No./Substance:
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0/Prostaglandins E; 53-84-9/NAD; EC 1.1.-/Alcohol Oxidoreductases; EC 1.1.1.-/Hydroxyprostaglandin Dehydrogenases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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