Synthesis and use of a lysolecithin analog for the purification of UDP-glucuronosyltransferase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference10 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. Effect of phospholipids on the thermal stability of microsomal UDP-glucuronosyltransferase
4. Synthesen von Cholinphosphatiden, V. Palmitoyl-propandiol-(1.3)-phosphorylcholin (2-Desoxylysolecithin) und ω.ω′-Alkandiol-Analoga
5. Regulation of Microsomal Enzymes by Phospholipids
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1. Microscale NMR Screening of New Detergents for Membrane Protein Structural Biology;Journal of the American Chemical Society;2008-05-14
2. Purification of a Phenobarbital-Inducible UDP-Glucuronosyltransferase Isoform from Dog Liver Which Catalyzes Morphine and Testosterone Glucuronidation;Archives of Biochemistry and Biophysics;1996-01
3. Isolation and identification of palmitoylphosphocholinepropanediol from γ-irradiated dipalmitoylphosphatidylcholine;Journal of the American Oil Chemists' Society;1993-08
4. Dietary Lipid Regulates the Amount and Functional State of UDP-Glucuronosyltransferase in Rat Liver;The Journal of Nutrition;1992-08-01
5. Effect of dietary lipids on levels of UDP-glucuronosyltransferase in liver;Biochemical Pharmacology;1992-07
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