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丙硫氧嘧啶及其前体与辣根过氧化物酶的相互作用。

Interaction of propylthiouracil and its precursors with horseradish peroxidase.

作者信息

Zaton A, Ochoa de Aspuru E

机构信息

Departamento de Bioquimica Colegio Universitario de Alava Universidad del Pais Vasco, Vitoria-Gasteiz, España.

出版信息

Biochem Biophys Res Commun. 1988 Jun 30;153(3):904-11. doi: 10.1016/s0006-291x(88)81313-5.

Abstract

Interactions of horseradish peroxidase with propylthiouracil, thiouracil, propyluracil and uracil lead to the formation of complexes that exhibit different absorption spectra which can be attributed to the perturbation of peroxidase as the result of the drug-binding on a polar site in the protein. In this paper, by dilatometry and viscometry structural alterations in horseradish peroxidase were detected from its interaction with propylthiouracil and thiouracil only, and the physiological inhibition of peroxidase for these antithyroid drugs seems to be through structural alterations in the protein.

摘要

辣根过氧化物酶与丙硫氧嘧啶、硫氧嘧啶、丙基尿嘧啶和尿嘧啶的相互作用会导致复合物的形成,这些复合物呈现出不同的吸收光谱,这可归因于药物结合在蛋白质的极性位点上对过氧化物酶的扰动。在本文中,仅通过膨胀计法和粘度测定法检测了辣根过氧化物酶与丙硫氧嘧啶和硫氧嘧啶相互作用引起的结构变化,而过氧化物酶对这些抗甲状腺药物的生理抑制作用似乎是通过蛋白质的结构变化实现的。

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