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Title: Attachment of substrate metabolite to prostaglandin H synthase upon reaction with arachidonic acid. Author: Kulmacz RJ. Journal: Biochem Biophys Res Commun; 1987 Oct 29; 148(2):539-45. PubMed ID: 3120709. Abstract: Prostaglandin H synthase was incubated with [14C]arachidonate and then analyzed by polyacrylamide gel electrophoresis under denaturing conditions and by high pressure liquid chromatography. A maximum of 1 mol of arachidonate metabolite was found to become attached per mol of synthase subunit in a time-dependent process that was much slower than the rate of self-catalyzed inactivation of the cyclooxygenase activity. Incubation of a mixture of the synthase and ovalbumin with [14C]arachidonate resulted in a selective attachment of radiolabel to the synthase. These results suggest the presence of a single site on the synthase that is susceptible to reaction with an arachidonate metabolite.[Abstract] [Full Text] [Related] [New Search]