MONOCLONAL-ANTIBODIES AGAINST 4-HYDROXYBIPHENYL-UDP-GLUCURONOSYLTRANSFERASE

Monoclonal antibodies against purified rat fiver 4-hydroxybiphenyl UDP-glucuronosyl-transferase were developed using the hybridoma technology. In immunoblot analysis the antibodies specifically reacted with purified 4-hydroxybiphenyl-UDPGT but not with other purified UDPGT enzyme fractions. One single band was detected with microsomes of rat fiver and small intestine but not with microsomes of kidney and lung. The reactive protein was also found in dog and human liver microsomes. It could be shown that there was no increase of immunoreactive protein after pretreatment with phenobarbital or 5,6-benzoflavone. This supports the hypothesis that more than one 4-hydroxybiphenyl-UDPGT exist in rat liver which are differently inducible.