Regulation of UDP-glucuronosyltransferase by lipid-protein interactions
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference22 articles.
1. A kinetic mechanism for modulation of the activity of microsomal UDP-glucuronyltransferase by phospholipids. Effects of lysophosphatidylcholines.
2. Factors modulating the catalytic specificity of a pure form of UDP-glucuronyltransferase.
3. Modulation of the number of ligand binding sites of UDP-glucuronyltransferase by the gel to liquid-crystal phase transition of phosphatidylcholines.
4. Evidence that UDP-glucuronyltransferase in liver microsomes at 37 degrees C is in a gel phase lipid environment.
5. Studies of the catalytic mechanism of microsomal UDP-glucuronyltransferase. Alpha-glucuronidase activity and its stimulation by phospholipids.
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2. Kinetic parameters of soil β-glucosidase response to environmental temperature and moisture regimes;Revista Brasileira de Ciência do Solo;2011-08
3. 4-AminobiphenylN-glucuronidation by liver microsomes: optimization of the reaction conditions and characterization of the UDP-glucuronosyltransferase isoforms;Journal of Applied Toxicology;2006
4. Gender-related differences in the amount and functional state of rat liver UDP-glucuronosyltransferase;Biochemical Pharmacology;1995-08
5. Dietary lipids induce Phase 2 enzymes in rat small intestine;Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism;1993-12
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