Attachment of substrate metabolite to prostaglandin H synthase upon reaction with arachidonic acid |
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Authors: | R J Kulmacz |
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Affiliation: | Department of Biological Chemistry, University of Illinois, Chicago 60680. |
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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. |
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