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. 1977 Sep;74(9):3691-5.
doi: 10.1073/pnas.74.9.3691.

Resolution of prostaglandin endoperoxide synthase and thromboxane synthase of human platelets

S Hammarström, P Falardeau

Resolution of prostaglandin endoperoxide synthase and thromboxane synthase of human platelets

S Hammarström et al. Proc Natl Acad Sci U S A. 1977 Sep.

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.

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References

    1. Prostaglandins. 1976 Dec;12(6):951-70 - PubMed
    1. Prostaglandins. 1976 Nov;12(5):811-28 - PubMed
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    1. J Biol Chem. 1976 Sep 25;251(18):5575-9 - PubMed
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