Ahlborg U G, Manzoor E, Thunberg T
Arch Toxicol. 1977 Jun 18;37(2):81-7. doi: 10.1007/BF00293856.
An earlier study of the metabolism of pentachlorophenol has shown that a metabolite, tetrachloro-p-hydroquinone, possessed pronounced inhibitory action on the activity of beta-glucuronidase from bacterial origin. Several other chlorinated hydroquinones and benzoquinones have now been studied with regard to their ability to inhibit beta-glucuronidase of various origin in vitro and in vivo. All the studied chlorinated hydroquinones and benzoquinones were found to be potent inhibitors of beta-glucuronidase of bacterial origin. D-glucaric acid-1.4-lactone was included for comparison and was found to be less active than the other studied compounds. The inhibition was found to be competitive in nature. No inhibitory effect of the benzo- and hydroquinones studied in vitro or in vivo could be demonstrated on beta-glucuronidase from livers. The result calls for precaution when using bacterial beta-glucuronidase to split urinary conjugates of glucuronic acid.
早期一项关于五氯苯酚代谢的研究表明,一种代谢物四氯对苯二酚对源自细菌的β-葡萄糖醛酸酶的活性具有显著抑制作用。现在已经对其他几种氯代对苯二酚和苯醌在体外和体内抑制各种来源的β-葡萄糖醛酸酶的能力进行了研究。发现所有研究的氯代对苯二酚和苯醌都是源自细菌的β-葡萄糖醛酸酶的有效抑制剂。加入D-葡糖二酸-1,4-内酯作为对照,发现其活性低于其他研究化合物。发现这种抑制本质上是竞争性的。在体外或体内研究的苯醌和对苯二酚对肝脏中的β-葡萄糖醛酸酶均未显示出抑制作用。该结果表明,在使用细菌β-葡萄糖醛酸酶分解尿中葡萄糖醛酸结合物时需要谨慎。