Abstract
Salicylic acid (SA), a weak inhibitor of the prostaglandin endoperoxide synthetase or fatty acid cyclooxygenase enzyme, is known to prevent irreversible enzyme inhibition by acetylsalicylic acid (ASA). The interaction of arachidonic acid with ferrous sulfate was used as a model to study the reaction of the fatty acid with the postulated enzymic cationic binding site on Fe2+-heme. SA was as potent as ASA in inhibiting the cooxygenation of arachidonic acid and ferrous sulfate. The result suggests that SA could compete effectively for the enzyme cationic site with ASA. Thus SA may block ASA acetylation of the cyclooxygenase by preventing ASA from binding to this site.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 161-164 |
| Number of pages | 4 |
| Journal | Prostaglandines and Medicine |
| Volume | 6 |
| Issue number | 2 |
| DOIs | |
| State | Published - Feb 1981 |
Bibliographical note
Funding Information:We gratefully acknowledge the support of USPHS grants HL-11880, AM-06317, HL-06314, CA-12607, CA-11996, GM-AM-22167, HL-20695, HL-16833, AM-15317, a grant from the Leukemia Task Force, and grant MA-7396 from the Medical Research Council of Canada. JMG is the recipient of a Canadian MRC scholarship and a grant from the Children's Hospital of Winnipeg Research Foundation.