Results 221 to 230 of about 25,599 (259)
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Biochemistry, 1986
Interfacial catalysis of hepatic triacylglycerol lipase (H-TGL) and lipoprotein lipase (LpL) isolated from human post-heparin plasma was investigated with mixed monolayers of trioleoylglycerol (TO) and egg phosphatidylcholine. Rates of enzyme catalysis were dependent on surface pressure, substrate concentration, apoC-II (the activator protein for LpL),
Richard L. Jackson +3 more
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Interfacial catalysis of hepatic triacylglycerol lipase (H-TGL) and lipoprotein lipase (LpL) isolated from human post-heparin plasma was investigated with mixed monolayers of trioleoylglycerol (TO) and egg phosphatidylcholine. Rates of enzyme catalysis were dependent on surface pressure, substrate concentration, apoC-II (the activator protein for LpL),
Richard L. Jackson +3 more
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Triacylglycerol Lipase in Developing Rat Sciatic Nerve
Journal of Neurochemistry, 1986Abstract: Triacylglycerol lipase activity, with a pH optimum of 7.5, was demonstrated in cell‐free homogenates of rat sciatic endoneurium. 1,2‐Diacylglycerol was the major product of triacylglycerol hydrolysis. A rapid decline in lipase activity was found in rats up to 2 months of age. After this time, the decrease continued, but at a much slower rate.
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Relevance of hepatic lipase to the metabolism of triacylglycerol-rich lipoproteins
Biochemical Society Transactions, 2003HL (hepatic lipase) is a glycoprotein that is synthesized and secreted by the liver, and which binds to heparan sulphate proteoglycans on the surface of sinusoidal endothelial cells and on the external surface of parenchymal cells in the space of Disse.
ZAMBON, ALBERTO +5 more
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Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1982
Highly purified rat hepatic lipase (NaCl-resistant, alkaline pH optimum) was studied to evaluate whether the enzyme has triacylglycerol lipase, monoacylglycerol lipase and phospholipase activities. Enzyme exhibiting a single band by SDS-polyacrylamide gel electrophoresis and having a specific activity eight times greater than that in any previous ...
Gordon L. Jensen +2 more
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Highly purified rat hepatic lipase (NaCl-resistant, alkaline pH optimum) was studied to evaluate whether the enzyme has triacylglycerol lipase, monoacylglycerol lipase and phospholipase activities. Enzyme exhibiting a single band by SDS-polyacrylamide gel electrophoresis and having a specific activity eight times greater than that in any previous ...
Gordon L. Jensen +2 more
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Immunochemical assay of rat postheparin plasma triacylglycerol lipases
Atherosclerosis, 1980Immunochemical methods for selective measurement of lipoprotein lipase and hepatic lipase activities in rat postheparin plasma are described and validated. Lipoprotein lipase was measured using a substrate containing 10% serum and 0.1 M NaCl after inactivation of hepatic lipase with a specific antiserum. Hepatic lipase was measured at 1.0 M NaCl with a
EskoA. Nikkilä +2 more
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Triacylglycerol lipase activities in tissues of Antarctic fishes
Polar Biology, 2002The activity of the lipolytic enzyme, triacylglycerol lipase (TAG lipase; E.C. 3.1.1.3) was measured in heart ventricle, liver, oxidative skeletal muscle, and adipose tissue of four species of Antarctic fishes (Chaenocephalus aceratus, Notothenia coriiceps, Trematomus newnesi, Gobionotothen gibberifrons).
Jeffrey R. Hazel, Bruce D. Sidell
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Fractionation of the triacylglycerols of lipase‐modified butter oil
Journal of the American Oil Chemists' Society, 1993AbstractTriacylglycerols (TGs) of lipase‐modified butter oil were separated into saturated, monoene, diene and triene fractions on ap‐propylbenzene sulfonic acid solid‐phase extraction column loaded with silver ions. Fatty acid analysis of the fractions showed that the amounts of saturated TGs (98.4 mol%) and monoene TGs (26.0 mol%) in the saturated ...
Paavo Kalo, Asmo Kemppinen
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Triacylglycerol hydrolysis by lipase in a flat membrane bioreactor
Biotechnology Techniques, 1994Hydrolysis of olive oil into fatty acids by lipase in a flat membrane module is reported. Lipase was immobilized by adsorption onto a hydrophilic cellulose acetate membrane. Hydrolysis was carried out by circulating pure olive on the enzyme side of the membrane and water phase on the other side. Conversion reached 85 % after 50 hours reaction time.
L. Szabó +3 more
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Purification of the intracellular triacylglycerol lipase ofOospora lactis
Chemistry of Natural Compounds, 1981A method for the isolation of homogeneous triacylglycerol hydrolase from the mycelium of the fungusOospora lactis is described. The homogeneity of the enzyme has been shown by gel filtration through Sephadex G-100, by ultracentrifugation, and by disc electrophoresis in polyacrylamide gel.
K. D. Davranov, M. I. Alimdzhanova
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Hydrolysis of triacylglycerol emulsions by lingual lipase a microscopic study
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1982The effect of lingual lipase on four different triacylglycerol emulsions was observed by light microscopy at pH 5-6. The extent of hydrolysis on the microscope slide was determined with the aid of radioactive emulsions or by analyzing the products by gas-liquid chromatography.
Margit Hamosh +4 more
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