Biomaterial Database

Extraction and partial purification of acyl-CoA:1-acyl-sn-glycero-3-phosphocholine acyltransferase from rat liver microsomes. 1980

H Hasegawa-Sasaki, and K Ohno

Acyl-CoA:1-acyl-sn-glycero-3-phosphocholine acyltransferase (EC 2.3.1.23) was extracted from rat liver microsomes with an aqueous dispersion of 1-acyl-sn-glycero-3-phosphocholine, a substrate of the enzyme, and purified up to 30-fold. The procedure includes removal of unrelevant proteins and lipids by washings of microsomes with a buffer of high ionic strength and with buffers containing detergents, extraction of the enzyme with an aqueous dispersion of 1-acyl-sn-glycero-3-phosphocholine, and chromatography by gel filtration. The acyltransferase was eluted from a Ultrogel AcA 34 column at a position with a Kav of 0.122; an elution position of a protein with a molecular weight of 225 000. The partially purified enzyme was active over a wide range of pH with an optimum at around pH 8. Depending on the acyl donors, different rates of the reaction were obtained by the preparation. The order was: arachidonoyl-CoA greater than linoleoyl-CoA = oleoyl-CoA greater than palmitoyl-CoA. The enzyme preparation acylated 1-acyl-sn-glycero-3-phosphocholine, 1-acyl-sn-glycero-3-phospho-ethanolamine and 1-acyl-sn-glycero-3-phosphoinositol but not acylated 2-acyl-sn-glycero-3-phosphocholine, 1-acyl-sn-glycerol 3-phosphate or diacylglycerol. Some sulfhydryl-binding reagents inactivated the enzyme.

UI	MeSH Term	Description	Entries
D008243	1-Acylglycerophosphocholine O-Acyltransferase	An enzyme localized predominantly within the plasma membrane of lymphocytes. It catalyzes the transfer of long-chain fatty acids, preferentially unsaturated fatty acids, to lysophosphatides with the formation of 1,2-diacylglycero-3-phosphocholine and CoA. EC 2.3.1.23.	1-Acylglycerophosphocholine Acyltransferase,Acyl CoA Lysolecithin Acyltransferase,Lysolecithin Acyltransferase,Acyl-CoA-1-Acylglycero-3-Phosphocholine-O-Acyltransferase,Lysophosphatidylcholine Acyltransferase,Lysophosphatidylcholine-Palmitoyl CoA Acyltransferase,Lysophospholipid Acyltransferase,1 Acylglycerophosphocholine Acyltransferase,1 Acylglycerophosphocholine O Acyltransferase,Acyl CoA 1 Acylglycero 3 Phosphocholine O Acyltransferase,Acyltransferase, 1-Acylglycerophosphocholine,Acyltransferase, Lysolecithin,Acyltransferase, Lysophosphatidylcholine,Acyltransferase, Lysophosphatidylcholine-Palmitoyl CoA,Acyltransferase, Lysophospholipid,CoA Acyltransferase, Lysophosphatidylcholine-Palmitoyl,Lysophosphatidylcholine Palmitoyl CoA Acyltransferase,O-Acyltransferase, 1-Acylglycerophosphocholine
D008297	Male		Males
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
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
D003902	Detergents	Purifying or cleansing agents, usually salts of long-chain aliphatic bases or acids, that exert cleansing (oil-dissolving) and antimicrobial effects through a surface action that depends on possessing both hydrophilic and hydrophobic properties.	Cleansing Agents,Detergent Pods,Laundry Detergent Pods,Laundry Pods,Syndet,Synthetic Detergent,Agent, Cleansing,Agents, Cleansing,Cleansing Agent,Detergent,Detergent Pod,Detergent Pod, Laundry,Detergent Pods, Laundry,Detergent, Synthetic,Detergents, Synthetic,Laundry Detergent Pod,Laundry Pod,Pod, Detergent,Pod, Laundry,Pod, Laundry Detergent,Pods, Detergent,Pods, Laundry,Pods, Laundry Detergent,Synthetic Detergents
D006358	Hot Temperature	Presence of warmth or heat or a temperature notably higher than an accustomed norm.	Heat,Hot Temperatures,Temperature, Hot,Temperatures, Hot
D006863	Hydrogen-Ion Concentration	The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH	pH,Concentration, Hydrogen-Ion,Concentrations, Hydrogen-Ion,Hydrogen Ion Concentration,Hydrogen-Ion Concentrations
D000217	Acyltransferases	Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.	Acyltransferase
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
D013379	Substrate Specificity	A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.	Specificities, Substrate,Specificity, Substrate,Substrate Specificities