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利用杆状病毒系统表达人血栓素合酶。

Expression of human thromboxane synthase using a baculovirus system.

作者信息

Yokoyama C, Miyata A, Suzuki K, Nishikawa Y, Yoshimoto T, Yamamoto S, Nüsing R, Ullrich V, Tanabe T

机构信息

Department of Pharmacology, National Cardiovascular Center Research Institute, Osaka, Japan.

出版信息

FEBS Lett. 1993 Feb 22;318(1):91-4. doi: 10.1016/0014-5793(93)81335-w.

Abstract

Human thromboxane (TX) synthase (EC 5.3.99.5) was produced by the baculovirus expression system using cDNA encoding human TX synthase [(1991) Biochem. Biophys. Res. Commun. 78, 1479-1484]. A recombinant baculovirus TXS7 was expressed in Spodoptera frugiperda Sf9 insect cells. The expressed protein was recognized by monoclonal antibody, Kon 7 raised against human TX synthase [(1990) Blood 76, 80-85]. The recombinant TX synthase catalyzed the conversion of prostaglandin (PG) H2 to TXA2 and 12-hydroxy-heptadecatrienoic acid (HHT). Both conversions of PGH2 to TXA2 and HHT by the expressed TX synthase were completely inhibited by a specific TX synthase inhibitor, OKY-046 (5 microM).

摘要

人血栓素(TX)合酶(EC 5.3.99.5)是通过杆状病毒表达系统利用编码人TX合酶的cDNA制备的[(1991年)《生物化学与生物物理研究通讯》78卷,第1479 - 1484页]。重组杆状病毒TXS7在草地贪夜蛾Sf9昆虫细胞中表达。表达的蛋白可被针对人TX合酶制备的单克隆抗体Kon 7识别[(1990年)《血液》76卷,第80 - 85页]。重组TX合酶催化前列腺素(PG)H2转化为血栓素A2(TXA2)和12 - 羟基 - 十七碳三烯酸(HHT)。表达的TX合酶将PGH2转化为TXA2和HHT的过程均被特异性TX合酶抑制剂OKY - 046(5微摩尔)完全抑制。

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