Unknown

Dataset Information

0

Studies on the purification of rat liver uridine diphosphate glucuronyltransferase.


ABSTRACT: 1. A stable, more highly purified, preparation of UDP-glucuronyltransferase was obtained than previously reported. 2. Enzyme activity towards o-aminophenyl and p-nitrophenyl was increased 43- and 46-fold respectively. 3. The final preparation contains only three staining polypeptide bands visible after sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. 4. The only known major accompanying protein appears to be epoxide hydratase. 5. The purified enzyme activity towards o-aminophenol can still be activated 3 fold by diethylnitrosamine. 6. On evidence from purification, o-aminophenol and p-nitrophenol appear to be glucuronidated by the same enzyme protein. The possible recognition of the UDP-glucuronyltransferase enzyme is discussed.

SUBMITTER: Burchell B 

PROVIDER: S-EPMC1164539 | biostudies-other | 1977 Mar

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1178020 | biostudies-other
| S-EPMC1184033 | biostudies-other
| S-EPMC1174163 | biostudies-other
| S-EPMC1178864 | biostudies-other
| S-EPMC1186469 | biostudies-other
| S-EPMC1178261 | biostudies-other
| S-EPMC1271242 | biostudies-other
| S-EPMC9299652 | biostudies-literature
| S-EPMC1185840 | biostudies-other
| S-EPMC1161858 | biostudies-other