Abstract
Bovine lung thromboxane synthase was immobilized on phenyl-Sepharose beads by adsorption. The immobilized enzyme was catalytically active and synthesized both TXA 2 and HHT. The structure-activity relationship of several hydroperoxy fatty acids and their ability to inactivate thromboxane synthase was investigated. Millimolar quantities of hydrogen peroxide and tert-butylperoxide were required to inactivate the enzyme; whereas micromolar quantities of C 18 and C 20 hydroperoxy fatty acids inactivated the enzyme. Pretreatment of the enzyme with long chain hydroperoxy-fatty acids resulted in a decreased synthesis of both TXB 2 and HHT.
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