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肝脏UDP-葡萄糖醛酸基转移酶活性的异质性:对参与对硝基苯酚葡萄糖醛酸化的同工酶的研究。

Heterogeneity of hepatic UDP-glucuronosyltransferase activities: investigations of isoenzymes involved in p-nitrophenol glucuronidation.

作者信息

Antoine B, Boutin J A, Siest G

机构信息

ICGM U129 INSERM 24, Paris, France.

出版信息

Comp Biochem Physiol C Comp Pharmacol Toxicol. 1993 Sep;106(1):241-8. doi: 10.1016/0742-8413(93)90278-s.

DOI:10.1016/0742-8413(93)90278-s
PMID:7903616
Abstract
  1. UDP-Glucuronosyltransferase (UGT, EC 2.1.4.17) has been measured routinely with para-nitrophenol (pNP) because the UGT assay using this substrate is easy to assess and run. 2. This compound has been used in several studies as a substrate for purification of the enzyme. 3. In the present work, we characterize the para-nitrophenol-conjugating activity. 4. An analysis of kinetics of para-nitrophenol conjugation obtained from various biological sources (various tissues and various species) leads us to the conclusion that at least three isoenzymes are responsible for this activity in the rat. 5. Both UGT-(testosterone) and the 3-methylcholanthrene-inducible form previously described in the literature, may be responsible for the activity, whilst a highly specific form (UGT-phenol) is reported here for the first time. 6. This work is intended to lay down the basis of further investigations, including purification of the highly specific isoform.
摘要
  1. 尿苷二磷酸葡萄糖醛酸基转移酶(UGT,EC 2.1.4.17)通常使用对硝基苯酚(pNP)进行测定,因为使用该底物的UGT测定易于评估和操作。2. 该化合物已在多项研究中用作酶纯化的底物。3. 在本研究中,我们对苯酚结合活性进行了表征。4. 对从各种生物来源(各种组织和各种物种)获得的对硝基苯酚结合动力学的分析使我们得出结论,大鼠体内至少有三种同工酶负责这种活性。5. UGT-(睾酮)和文献中先前描述的3-甲基胆蒽诱导型可能都负责这种活性,而这里首次报道了一种高度特异性的形式(UGT-苯酚)。6. 这项工作旨在为进一步的研究奠定基础,包括纯化高度特异性的同工型。

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