| 内容提要: |
We tested whether the UGT-Glo substrate A can be used for the determination of glucosidation activity in addition to its well-known property as a glucuronidation substrate. The UGT enzyme of choice here was UGT2B7 while for comparison, UGT1A9 and HLMs were also tested. Both of them by far most common polymorphic variants of UGT2B7 were able to efficiently catalyze the glucosidation of the luminogenic substrate, while HLMs were much less effective (likely due to a lower content of UGT2B7) and UGT1A9 was essentially negative. These data show for the first time that the UGT-Glo substrate A is a useful probe for the study of UGT-dependent glucosidation. |