Green M D, Coffman B L, Irshaid Y M, Tephly T R
Department of Pharmacology, University of Iowa, Iowa City 52242.
Arch Biochem Biophys. 1988 Apr;262(1):367-74. doi: 10.1016/0003-9861(88)90200-7.
An antibody to a UDP-glucuronosyltransferase (UDPGT) isoenzyme which catalyzes the glucuronidation of p-nitrophenol (PNP) in rabbit liver was raised in sheep and used to identify immunologically similar UDPGTs in rabbit and human livers. Immunoblotting experiments showed that the antisera specifically recognized PNP UDPGT but not estrone UDPGT purified from rabbit liver. Sheep anti-rabbit liver PNP UDPGT IgG immunoprecipitated PNP, 1-naphthol, and 4-methylumbelliferone glucuronidation activities in rabbit and human liver microsomal preparations. In rabbit liver microsomes the antibody did not immunoprecipitate estrone or estradiol glucuronidation activities. In human liver microsomes, 4-aminobiphenyl but not estriol glucuronidation activities were immunoprecipitated, suggesting that the antibody recognizes a specific UDPGT (pI 6.2) in human liver microsomes.
一种针对兔肝脏中催化对硝基苯酚(PNP)葡萄糖醛酸化的尿苷二磷酸葡萄糖醛酸基转移酶(UDPGT)同工酶的抗体在绵羊体内产生,并用于鉴定兔和人肝脏中免疫相似的UDPGT。免疫印迹实验表明,抗血清能特异性识别PNP UDPGT,但不能识别从兔肝脏中纯化的雌酮UDPGT。绵羊抗兔肝脏PNP UDPGT IgG在兔和人肝脏微粒体制剂中免疫沉淀PNP、1-萘酚和4-甲基伞形酮葡萄糖醛酸化活性。在兔肝脏微粒体中,该抗体不能免疫沉淀雌酮或雌二醇葡萄糖醛酸化活性。在人肝脏微粒体中,4-氨基联苯的葡萄糖醛酸化活性可被免疫沉淀,而雌三醇的葡萄糖醛酸化活性则不能,这表明该抗体识别的是人类肝脏微粒体中的一种特定UDPGT(pI 6.2)。