人血小板中前列腺素内过氧化物合酶和血栓素合酶的解析
Resolution of prostaglandin endoperoxide synthase and thromboxane synthase of human platelets.
作者信息
Hammarström S, Falardeau P
出版信息
Proc Natl Acad Sci U S A. 1977 Sep;74(9):3691-5. doi: 10.1073/pnas.74.9.3691.
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.
摘要
血栓素合酶定位于人血小板的微粒体中。该酶对巯基试剂和硫醇不敏感，但被12L-氢过氧-5,8,10,14-二十碳四烯酸抑制（50%抑制浓度 = 0.1 mM）。用 Triton X-100处理微粒体可溶解催化花生四烯酸转化为血栓素B2的酶。溶解后的物质通过DEAE-纤维素色谱法分离为两个组分，一个将花生四烯酸转化为前列腺素G2和H2，另一个将前列腺素H2转化为血栓素B2。
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