将纯化的Wistar大鼠肝脏胆红素UDP-葡萄糖醛酸基转移酶重组到Gunn大鼠肝脏微粒体中。
Reconstitution of purified Wistar rat liver bilirubin UDP-glucuronyltransferase into Gunn-rat liver microsomes.
作者信息
Burchell B
出版信息
Biochem J. 1982 Mar 1;201(3):653-6. doi: 10.1042/bj2010653.
Abstract
- Reconstitution of purified bilirubin UDP-glucuronyltransferase from Wistar-rat liver into Gunn-rat liver microsomes provides a better environment than phosphatidylcholine liposomes, such that the final specific activity of the Wistar-rat liver enzyme was increased up to 85 units/mg of protein. 2. Gunn- and Wistar-rat liver microsomes were equally effective for reconstitution of the purified enzyme. 3. The transferase activity does not appear to be fully expressed in the more rigid environment of foetal Wistar-rat liver microsomes. 4. These reconstitution experiments reveal a final specific activity for the purified bilirubin UDP-glucuronyltransferase consistent with the capacity of the whole rat liver to glucuronidate bilirubin and indicate that the absence of this enzyme activity in Gunn-rat liver microsomes is not due to an abnormal microenvironment.
摘要
- 将来自Wistar大鼠肝脏的纯化胆红素UDP-葡萄糖醛酸基转移酶重组到Gunn大鼠肝脏微粒体中，比磷脂酰胆碱脂质体提供了更好的环境，使得Wistar大鼠肝脏酶的最终比活性提高到85单位/毫克蛋白质。2. Gunn大鼠和Wistar大鼠肝脏微粒体在重组纯化酶方面同样有效。3. 在胎儿Wistar大鼠肝脏微粒体更刚性的环境中，转移酶活性似乎未完全表达。4. 这些重组实验揭示了纯化胆红素UDP-葡萄糖醛酸基转移酶的最终比活性与整个大鼠肝脏将胆红素葡萄糖醛酸化的能力一致，并表明Gunn大鼠肝脏微粒体中这种酶活性的缺失不是由于异常的微环境。
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本文引用的文献
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Isolation and purification of bilirubin UDP-glucuronyl-transferase from rat liver.从大鼠肝脏中分离纯化胆红素UDP-葡萄糖醛酸基转移酶。
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