Production of platelet thromboxane A2 inactivates purified human platelet thromboxane synthase.
Production of platelet thromboxane A2 inactivates purified human platelet thromboxane synthase.
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血小板血栓素 A2 的产生会使纯化的人血小板血栓素合酶失活。
DOI：
10.1042/bj2330637
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
Venton,DL
中科院分区：
文献类型：
--
作者：
Hall,ER;Tuan,WM;Venton,DL
采用DEAE-cellulose、Affi-Gel Blue和Sephacryl S-300层析对人血小板血栓素合成酶进行了部分纯化，其比活性为259 nmol的血栓素B2/min / mg.当与苯基- sepharose结合时，血栓素合成酶保留了75-90%的酶活性。固定化酶在pH 3.0下失活，并被1-苯并咪唑和U-63,557A抑制。这种酶从前列腺素H2生成血栓素A2的能力由于多次添加前列腺素H2而显著降低。我们的数据表明，酶产生血栓素A2是自我限制的，酶在反应过程中失活。
Human platelet thromboxane synthase was partially purified by DEAE-cellulose, Affi-Gel Blue, and Sephacryl S-300 chromatography to a specific activity of 259 nmol of thromboxane B2/min per mg. Thromboxane synthase retained 75-90% of its enzymic activity when bound to phenyl-Sepharose. The immobilized enzyme was inactivated at pH 3.0 and inhibited by 1-benzylimidazole and U-63,557A. The ability of the enzyme to produce thromboxane A2 from prostaglandin H2 was dramatically reduced by multiple additions of prostaglandin H2. Our data suggest that the production of thromboxane A2 by the enzyme is self-limiting and that the enzyme is inactivated during the reaction.