Disulfide bond-mediated stabilization of the oligomers of UDP-glucuronosyltransferase 2B7.

ABSTRACT: UDP-glucuronosyltransferase (UGT) is an important drug-metabolizing enzyme involved in the detoxification of hydrophobic chemicals by conjugating them with hydrophilic glucuronic acid. Previous studies have revealed that UGTs form oligomers between or among the same or other isoforms, but the molecular mechanism underlying this formation remains unclear. In this study, we used optimized electrophoretic techniques to analyze UGT2B7 homo-oligomer formation. UGT2B7 was expressed in COS-1 cells, and lysates were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). By omitting the heating and reducing steps during SDS-PAGE sample preparation, bands corresponding to dimer, tetramer, and higher-order oligomers were detected in addition to monomeric bands. Since these

SUBMITTER: Miyauchi Y 

PROVIDER: S-EPMC12390933 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature