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联苯甲酰,一种在体外对微粒体环氧化物水解酶有强效激活作用的物质。

Benzil, a potent activator of microsomal epoxide hydrolase in vitro.

作者信息

Seidegård J, DePierre J W

出版信息

Eur J Biochem. 1980 Dec;112(3):643-8. doi: 10.1111/j.1432-1033.1980.tb06129.x.

Abstract

Benzil was found to be a very potent activator of microsomal epoxide hydrolase activity (measured with styrene oxide as substrate) in vitro. The activating effect was uncompetitive and benzil causes approximately ninefold increases in both the apparent V and the apparent Km of the enzyme(s). The half-maximal effect on activity was obtained as a 0.3 mM concentration of benzil. The activating effect obtained with benzil was found to be very specific, since a variety of structurally related compounds had little or no effect on microsomal epoxide hydrolase activity. In order to obtain indications for the existence of more than one microsomal epoxide hydrolase the effect of benzil on this activity from rats induced with phenobarbital, 3-methylcholanthrene, 2-acetylaminofluorene, trans-stilbene oxide, and benzil was tested. The differences observed were minor.

摘要

已发现苯偶酰在体外是微粒体环氧化物水解酶活性(以氧化苯乙烯为底物进行测定)的一种非常有效的激活剂。激活作用是非竞争性的,且苯偶酰使该酶的表观V和表观Km均增加约9倍。在苯偶酰浓度为0.3 mM时获得对活性的半数最大效应。发现苯偶酰产生的激活作用具有高度特异性,因为多种结构相关化合物对微粒体环氧化物水解酶活性几乎没有影响。为了获得存在不止一种微粒体环氧化物水解酶的迹象,测试了苯偶酰对用苯巴比妥、3-甲基胆蒽、2-乙酰氨基芴、反式氧化 stilbene和苯偶酰诱导的大鼠的这种活性的影响。观察到的差异很小。

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