CONFORMATIONAL-CHANGES OF PEROXIDASE AND ALBUMIN IN SOLUTIONS OF PROPYLTHIOURACIL

被引：6

作者：

ZATON, A

FERNANDEZ, R

ZABALLA, O

机构：

[1] Departamento de Bioquimica, Universidad del Pais Vasco, Facultad de Farmacia, Vitoria-Gasteiz

来源：

BIOCHEMICAL PHARMACOLOGY | 1990年 / 40卷 / 03期

关键词：

D O I：

10.1016/0006-2952(90)90550-5

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

Conformational changes of peroxidase and albumin in buffered solutions of propylthiouracil, an antithyroid drug, were evaluated by dilatometry and viscometry, showing that the structural alteration of peroxidase is related to the decoupling of the reactions which it catalyses. Thus, propylthiouracil probably inactivates the peroxidase by altering its structure. Equilibrium dialysis showed that albumin is the principle propylthiouracil-transporting protein in human serum. Propylthiouracil induces a conformational change in albumin when 1 mole of drug per mole of protein is bound, a structural alteration that can change the binding capability of other ligands. © 1990.

引用

页码：515 / 519

页数：5

共 30 条

[21] STUDIES OF BIOSYNTHESIS OF THYROXINE .2. SOLUBILIZATION AND CHARACTERIZATION OF AN IODIDE PEROXIDASE FROM THYROID TISSUE [J].