title: Resolution of prostaglandin endoperoxide synthase and thromboxane synthase of human platelets.
abstract: Thromboxane synthase was localized to the microsomes of human platelets. The enzyme was insensitive to sulfhydryl reagents and thiols but was inhibited by 12L-hydroperoxy-5, 8, 10, 14-eicosatetraenoic acid (concentration for 50% inhibition = 0.1 mM). Treatment of microsomes with Triton X-100 solubilized the enzymes that catalyze the conversion of arachidonic acid to thromboxane B2. The solubilized material was resolved by DEAE-cellulose chromatography into two components, one converting arachidonic acid to prostaglandins G2 and H2 and the other converting prostaglandin H2 to thromboxane B2.
mesh_terms: D001792:Blood Platelets / Q000201:enzymology*; D006801:Humans; D007700:Kinetics; D010088:Oxidoreductases / Q000097:blood*; D011449:Prostaglandin Endoperoxides; D011451:Prostaglandin-Endoperoxide Synthases / Q000097:blood* / Q000302:isolation & purification; D013347:Subcellular Fractions / Q000201:enzymology; D013930:Thromboxane-A Synthase / Q000097:blood* / Q000302:isolation & purification
chemical_list: D011449:Prostaglandin Endoperoxides; D010088:Oxidoreductases; D011451:Prostaglandin-Endoperoxide Synthases; D013930:Thromboxane-A Synthase