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Title: Resolution of prostaglandin endoperoxide synthase and thromboxane synthase of human platelets. Author: Hammarström S, Falardeau P. Journal: Proc Natl Acad Sci U S A; 1977 Sep; 74(9):3691-5. PubMed ID: 410024. 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.[Abstract] [Full Text] [Related] [New Search]