大鼠肝脏中尿苷二磷酸葡萄糖醛酸基转移酶的异质性。
The heterogeneity of uridine diphosphate glucuronyltransferase from rat liver.
作者信息
Mulder G J
出版信息
Biochem J. 1971 Nov;125(1):9-15. doi: 10.1042/bj1250009.
Abstract
- The glucuronide conjugation of p-nitrophenol, phenolphthalein, o-aminophenol and 4-methylumbelliferone by rat liver microsomes has been studied. The detergent Triton X-100 activated UDP-glucuronyltransferase activity towards all these substrates, therefore the optimum activating concentration was added in all experiments. 2. Mg(2+) enhanced the conjugation of the substrates. 3. With phenolphthalein substrate inhibition occurred but this could be relieved by adding albumin, which binds excess of phenolphthalein. 4. Kinetic constants of the substrates and UDP-glucuronate have been determined. Mutual inhibition was found with the substrates p-nitrophenol, 4-methylumbelliferone and phenolphthalein. p-Nitrophenol conjugation was inhibited competitively by phenolphthalein and 4-methylumbelliferone. 5. o-Aminophenol did not inhibit the conjugation of the other three substrates because these are conjugated preferentially to o-aminophenol. 6. It is concluded that the four substrates are conjugated by one enzyme at the same active site.
摘要
- 已对大鼠肝微粒体对对硝基苯酚、酚酞、邻氨基酚和4-甲基伞形酮的葡萄糖醛酸结合反应进行了研究。去污剂Triton X-100可激活UDP-葡萄糖醛酸转移酶对所有这些底物的活性，因此在所有实验中均加入了最佳激活浓度。2. Mg(2+)增强了底物的结合反应。3. 对于酚酞底物存在抑制作用，但加入可结合过量酚酞的白蛋白可缓解这种抑制。4. 已测定了底物和UDP-葡萄糖醛酸的动力学常数。发现对硝基苯酚、4-甲基伞形酮和酚酞这几种底物之间存在相互抑制作用。酚酞和4-甲基伞形酮竞争性抑制对硝基苯酚的结合反应。5. 邻氨基酚不抑制其他三种底物的结合反应，因为这些底物优先与邻氨基酚结合。6. 得出结论：这四种底物由同一种酶在同一活性位点进行结合反应。
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