Coughtrie M W, Burchell B, Leakey J E, Hume R
Department of Biochemistry, The University, Dundee, Scotland.
Mol Pharmacol. 1988 Dec;34(6):729-35.
Two anti-rat UDP-glucuronosyltransferase (UDPGT) antibody preparations, exhibiting different specificity of recognition of UDPGT isoenzymes on immunoblot analysis, were used to investigate the molecular basis of the perinatal inadequacy of glucuronidation in rats and humans. Immunoblot analysis of microsomes from developing rat liver demonstrated that the deficiency in bilirubin and testosterone glucuronidation in the fetus was due to the absence of the UDPGT isoenzyme proteins responsible for these conjugations. In contrast, phenol UDPGT enzyme activity and protein was detectable in significant amounts in fetal rat liver (greater than 30% of adult levels). In human liver, only one major immunoreactive polypeptide was observed in fetal microsomes. The remaining UDPGTs present in adult human liver developed postnatally, in parallel with the appearance of enzyme activities. Therefore, there was a correlation between the development of enzyme activity and enzyme protein. The possible consequences of developmental inadequacy of conjugation reactions for the fetus is discussed.
使用两种抗大鼠尿苷二磷酸葡萄糖醛酸转移酶（UDPGT）抗体制剂，它们在免疫印迹分析中对UDPGT同工酶的识别具有不同的特异性，以研究大鼠和人类围产期葡萄糖醛酸化不足的分子基础。对发育中的大鼠肝脏微粒体进行免疫印迹分析表明，胎儿中胆红素和睾酮葡萄糖醛酸化的缺乏是由于负责这些结合的UDPGT同工酶蛋白的缺失。相比之下，在胎鼠肝脏中可检测到大量的苯酚UDPGT酶活性和蛋白质（大于成年水平的30%）。在人肝脏中，在胎儿微粒体中仅观察到一种主要的免疫反应性多肽。成人肝脏中存在的其余UDPGT在出生后发育，与酶活性的出现同步。因此，酶活性的发展与酶蛋白之间存在相关性。讨论了结合反应发育不足对胎儿可能产生的后果。
