Characterization of antibodies to a rabbit hepatic UDP-glucuronosyltransferase and the identification of an immunologically similar enzyme in human liver.
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.
D000818:Animals; D000906:Antibodies / Q000032:analysis*; D003429:Cross Reactions; D014453:Glucuronosyltransferase / Q000032:analysis / Q000276:immunology*; D006801:Humans; D007163:Immunosorbent Techniques; D007526:Isoelectric Point; D007527:Isoenzymes / Q000032:analysis; D008099:Liver / Q000201:enzymology*; D009596:Nitrophenols / Q000378:metabolism; D011817:Rabbits; D012756:Sheep
D000906:Antibodies; D007527:Isoenzymes; D009596:Nitrophenols; D014453:Glucuronosyltransferase; C024836:4-nitrophenol