Zaleski J, Gessner T
Res Commun Chem Pathol Pharmacol. 1982 Aug;37(2):279-92.
Specific activities of UDP-glucuronosyltransferase and glucose-6-phosphatase, a marker enzyme of endoplasmic reticulum, were measured in mitochondria and microsomes. In mitochondria the specific activity of UDP-glucuronosyltransferase represented only 7-11% of that found in microsomes, when measured in the presence of various aglycone substrates, including 4-nitrophenol, 4-methylumbelliferone, 1-naphthol, phenolphthalein, testosterone and 17 beta-estradiol. Similarly, the specific activity of glucose-6-phosphatase in mitochondrial preparations was about 80% of that found in microsomes. In conclusion, it seems that in rat liver the UDP-glucuronosyltransferase activity associated with mitochondrial fractions reflects the presence of membrane fragments derived from endoplasmic reticulum, rather than mitochondrial location of this enzyme.
在内质网的一种标志酶——尿苷二磷酸葡萄糖醛酸基转移酶（UDP - 葡萄糖醛酸基转移酶）和葡萄糖 - 6 - 磷酸酶的比活性在线粒体和微粒体中进行了测定。当在包括4 - 硝基苯酚、4 - 甲基伞形酮、1 - 萘酚、酚酞、睾酮和17β - 雌二醇等各种糖苷配基底物存在的情况下进行测量时，线粒体中UDP - 葡萄糖醛酸基转移酶的比活性仅为微粒体中的7 - 11%。同样，线粒体制剂中葡萄糖 - 6 - 磷酸酶的比活性约为微粒体中的80%。总之，在大鼠肝脏中，与线粒体部分相关的UDP - 葡萄糖醛酸基转移酶活性似乎反映了源自内质网的膜片段的存在，而非该酶在线粒体中的定位。
