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PMID: 404672 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Lack of covalent modification of prostaglandin synthetase (cyclo-oxygenase) by indomethacin.

Prostaglandins ·Vol. 13 ·No. 4 ·1977-04-00 ·Pages 669-75

Stanford N, Roth GJ, Shen TY, Majerus PW

Abstract

We have previously shown that aspirin irreversibly inhibits prostaglandin synthetase (cyclo-oxygenase) by acetylating the active site of the enzyme. By utilizing 14C-labeled indomethacin and a close analogue, we now show that indomethacin, unlike aspirin, does not covalently modify cyclo-oxygenase. Furthermore, indomethacin binding to the enzyme may be reversible since even though indomethacin can inhibit acetylation by aspirin, when enzyme inhibited by indomethacin (1 micronM) is treated with 200 micronM aspirin 3 times for 1 hour each, complete acetylation of cyclo-oxygenase is achieved.

MeSH Terms
Acetylation Aspirin/metabolism,pharmacology Binding Sites/drug effects Drug Synergism Indomethacin/analogs & derivatives,metabolism,pharmacology Mixed Function Oxygenases/metabolism Prostaglandin-Endoperoxide Synthases/metabolism Protein Binding/drug effects
Chemicals
Mixed Function Oxygenases Prostaglandin-Endoperoxide Synthases Aspirin Indomethacin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Stanford N
Roth G J
Shen T Y
Majerus P W
Article Info
Journal
Prostaglandins
Abbr.
Prostaglandins
ISSN
0090-6980
Published
1977-04-00
Pages
669-75
Language
English
Region
United States
NLM ID
0320271
Subset
IM
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