Biomaterial Database

Delipidation and reactivation of UDPglucuronosyltransferase from rat liver. 1975

P L Jansen, and I M Arias

UDPglucuronosyltransferase was solubilized by treating Wistar rat liver microsomes with deoxycholate. Chromatography of this preparation on Bio-Gel P-30 resulted in extraction of 92% of phospholipids and complete loss of enzyme activity. UDPglucuronosyltransferase was reactivated by dialysing this delipidated preparation in the presence of lecithin, a mixture of liver microsomal lipids or microsomal preparations from livers of UDPglucuronosyltransferase-deficient Gunn rats. Virtually complete enzyme reactivation was obtained with regard to glucuronidation and glucosidation of bilirubin; however, the inactivation of UDPglucuronosyltransferase with p-nitrophenol as substrate was irreversible. These findings demonstrate that UDPglucuronosyltransferase with bilirubin as substrate is a lipid-requiring enzyme.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D008862	Microsomes, Liver	Closed vesicles of fragmented endoplasmic reticulum created when liver cells or tissue are disrupted by homogenization. They may be smooth or rough.	Liver Microsomes,Liver Microsome,Microsome, Liver
D009596	Nitrophenols	PHENOLS carrying nitro group substituents.	Nitrophenol
D010713	Phosphatidylcholines	Derivatives of PHOSPHATIDIC ACIDS in which the phosphoric acid is bound in ester linkage to a CHOLINE moiety.	Choline Phosphoglycerides,Choline Glycerophospholipids,Phosphatidyl Choline,Phosphatidyl Cholines,Phosphatidylcholine,Choline, Phosphatidyl,Cholines, Phosphatidyl,Glycerophospholipids, Choline,Phosphoglycerides, Choline
D011485	Protein Binding	The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.	Plasma Protein Binding Capacity,Binding, Protein
D011489	Protein Denaturation	Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.	Denaturation, Protein,Denaturations, Protein,Protein Denaturations
D002850	Chromatography, Gel	Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.	Chromatography, Exclusion,Chromatography, Gel Permeation,Chromatography, Molecular Sieve,Gel Filtration,Gel Filtration Chromatography,Chromatography, Size Exclusion,Exclusion Chromatography,Gel Chromatography,Gel Permeation Chromatography,Molecular Sieve Chromatography,Chromatography, Gel Filtration,Exclusion Chromatography, Size,Filtration Chromatography, Gel,Filtration, Gel,Sieve Chromatography, Molecular,Size Exclusion Chromatography
D003840	Deoxycholic Acid	A bile acid formed by bacterial action from cholate. It is usually conjugated with glycine or taurine. Deoxycholic acid acts as a detergent to solubilize fats for intestinal absorption, is reabsorbed itself, and is used as a choleretic and detergent.	Deoxycholate,Desoxycholic Acid,Kybella,Choleic Acid,Deoxycholic Acid, 12beta-Isomer,Deoxycholic Acid, 3beta-Isomer,Deoxycholic Acid, 5alpha-Isomer,Deoxycholic Acid, Disodium Salt,Deoxycholic Acid, Magnesium (2:1) Salt,Deoxycholic Acid, Monoammonium Salt,Deoxycholic Acid, Monopotassium Salt,Deoxycholic Acid, Monosodium Salt,Deoxycholic Acid, Sodium Salt, 12beta-Isomer,Dihydroxycholanoic Acid,Lagodeoxycholic Acid,Sodium Deoxycholate,12beta-Isomer Deoxycholic Acid,3beta-Isomer Deoxycholic Acid,5alpha-Isomer Deoxycholic Acid,Deoxycholate, Sodium,Deoxycholic Acid, 12beta Isomer,Deoxycholic Acid, 3beta Isomer,Deoxycholic Acid, 5alpha Isomer
D006602	Hexosyltransferases	Enzymes that catalyze the transfer of hexose groups. EC 2.4.1.-.
D000818	Animals	Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA.	Animal,Metazoa,Animalia