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[人胎盘谷胱甘肽-S-转移酶的物理化学性质及催化特性的初步研究]

[Preliminary study of the physical chemistry and catalytic properties of glutathione-S-transferase from human placenta].

作者信息

Polidoro G, Zulli P, Di Ilio C, Del Boccio G, Di Cola D, Federici G

出版信息

Boll Soc Ital Biol Sper. 1979 May 15;55(9):840-3.

PMID:553608
Abstract

Glutathione-S-transferase activity has been identified in the cytosol of human placenta. The specific activity measured is about 50% of that found in human liver. While some kinetic data have a close correspondence with those attributed to transferases of other sources, the molecular weight (60.000 daltons) and electric properties of this protein are unusual. The inhibitory effect of several non-substrate compounds suggests that also the placental Glutathione-S-transferase may play some role in detoxication of exogenous substances.

摘要

已在人胎盘的胞质溶胶中鉴定出谷胱甘肽 - S - 转移酶活性。所测得的比活性约为人肝脏中该酶比活性的50%。虽然一些动力学数据与其他来源的转移酶的数据密切对应,但这种蛋白质的分子量(60,000道尔顿)和电学性质却不同寻常。几种非底物化合物的抑制作用表明,胎盘谷胱甘肽 - S - 转移酶在外源性物质的解毒过程中也可能发挥一定作用。

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