Abstract
1. Nuclear, nuclear-envelope and microsomal preparations were prepared from rat liver, and their purity and morphology monitored by electron microscopy. 2. UDP-glucuronosyltransferase activity in microsomal preparations, but not in standard nuclear or nuclear-envelope preparations, displays latency from the criterion of being enhanced ('activated') by a range of detergents or the endogenous activator UDP-N-acetyl-glucosamine. 3. Nuclear preparations resemble activated rather than native microsomal preparations in failing to transfer glucuronic acid from 4-nitrophenyl glucuronide to 2-aminophenol. 4. Electron microscopy indicates that membranes of nuclear preparations and of our standard nuclear-envelope preparations remain, as in vivo, in a cisternal arrangement, whereas those of microsomal preparations are vesiculated. 5. In nuclear-envelope preparations in which vesiculation has been encouraged, the transferase can be activated by detergents. 6. We suggest that latency of UDP-glucuronosyltransferase results from vesiculation of membranes during preparation and that the latency of the microsomal transferase is largely a preparative artefact.
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- Berry C., Hallinan T. 'Coupled transglucuronidation': a new tool for studying the latency of UDP-glucuronyl transferase. FEBS Lett. 1974 May 15;42(1):73–76. doi: 10.1016/0014-5793(74)80282-6. [DOI] [PubMed] [Google Scholar]
- Berry C., Hallinan T. Summary of a novel, three-component regulatory model for uridine diphosphate glucuronyltransferase. Biochem Soc Trans. 1976;4(4):650–652. doi: 10.1042/bst0040650. [DOI] [PubMed] [Google Scholar]
- Fry D. J., Wishart G. J. Apparent induction by phenobarbital of uridine diphosphate glucuronyltransferase activity in nuclear envelopes of embryonic-chick liver. Biochem Soc Trans. 1976;4(2):265–266. doi: 10.1042/bst0040265. [DOI] [PubMed] [Google Scholar]
- Gunderson H. M., Nordlie R. C. The fully-active nature of synthetic and hydrolytic activities of glucose-6-phosphatase of intact nuclear membrane. Biochem Biophys Res Commun. 1973 May 15;52(2):601–607. doi: 10.1016/0006-291x(73)90755-9. [DOI] [PubMed] [Google Scholar]
- Kay R. R., Fraser D., Johnston I. R. A method for the rapid isolation of nuclear membranes from rat liver. Characterisation of the membrane preparation and its associated DNA polymerase. Eur J Biochem. 1972 Oct 17;30(1):145–154. doi: 10.1111/j.1432-1033.1972.tb02081.x. [DOI] [PubMed] [Google Scholar]
- LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
- Nilsson O. S., DePierre J. W., Dallner G. Investigation of the transverse topology of the microsomal membrane using combinations of proteases and the non-penetrating reagent diazobenzene sulfonate. Biochim Biophys Acta. 1978 Jul 20;511(1):93–104. doi: 10.1016/0005-2736(78)90067-6. [DOI] [PubMed] [Google Scholar]
- Otani G., Abou-El-Makarem M. M., Bock K. W. UDP-glucuronyltransferase in perfused rat liver and in microsomes - III. Effects of galactosamine and carbon tetrachloride on the glucuronidation of 1-naphthol and bilirubin. Biochem Pharmacol. 1976 Jun 1;25(11):1293–1297. doi: 10.1016/0006-2952(76)90092-7. [DOI] [PubMed] [Google Scholar]
- Weibel E. R., Stäubli W., Gnägi H. R., Hess F. A. Correlated morphometric and biochemical studies on the liver cell. I. Morphometric model, stereologic methods, and normal morphometric data for rat liver. J Cell Biol. 1969 Jul;42(1):68–91. doi: 10.1083/jcb.42.1.68. [DOI] [PMC free article] [PubMed] [Google Scholar]

