Results 211 to 220 of about 25,599 (259)

Triacylglycerol lipase activity in the rabbit renal medulla

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1987
Although the renal medulla is rich in triacylglycerols, the lipolysis of these intracellular triacylglycerols by a renomedullary triacylglycerol lipase has not been directly demonstrated. The present study demonstrates triacylglycerol lipase activity localized in the particulate subcellular fractions of rabbit renal medullae.
Theodore E. Liston, Alberto Nasjletti
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Regulation and function of triacylglycerol lipases in cellular metabolism

Biochemical Journal, 2008
The ability to store energy in the form of energy-dense TAG (triacylglycerol) and to mobilize these stores rapidly during times of low carbohydrate availability (fasting or famine) or during heightened metabolic demand (exercise or cold-stress) is a highly conserved process essential for survival. Today, in the presence of nutrient excess and sedentary
Matthew J. Watt, Gregory R. Steinberg
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Some properties of triacylglycerol lipase in chicken erythrocytes

International Journal of Biochemistry, 1986
Membrane-bound acid lipase was found in the chicken erythrocytes ghosts, having an optimum pH of 4.5. The membrane-bound lipase showed its maximum activity at 38 degrees C, and it was stable below 45 degrees C. The bound lipase was activated by octyl glucoside and 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (CHAPS), but it was markedly ...
Makato Fujii, Takao Fukunaga, Shiho Nishisako, Katsuya Koga   +3 more
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Identification of a triacylglycerol lipase in the diatom Phaeodactylum tricornutum

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2016
Diatoms accumulate triacylglycerols (TAGs) as storage lipids, but the knowledge about the molecular mechanisms of lipid metabolism is still sparse. Starting from a partial sequence for a putative TAG-lipase of the diatom Phaeodactylum tricornutum retrieved from the data bases, we have identified the full length coding sequence, tgl1.
Helge B. Bode, Wolfram Lorenzen, Tilman Ahrendt, Claudia Büchel, Max Angstenberger, Frederik Barka   +5 more
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Hydrolysis of synthetic triacylglycerols by pancreatic and lipoprotein lipase

Lipids, 1974
AbstractThe stereochemical course of the hydrolysis of synthetic sn‐glycerol‐1‐palmitate‐2‐oleate‐3‐linoleate, sn‐glycerol‐1,2‐dipalmitate‐3‐oleate and their antipodes by pancreatic and milk lipoprotein lipase was investigated by thin layer and gas liquid chromatographies of the diacylglycerol intermediates.
Dmytro Buchnea, N. H. Morley, Arnis Kuksis   +2 more
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Mechanistic model for the lipase-catalyzed alcoholysis of triacylglycerols [PDF]

Applied Catalysis A: General, 2006
Abstract The enzymatic alcoholysis of triolein and an oil highly rich in polyunsaturated fatty acid with ethanol to obtain 2-monoacylglycerols (2-MG) was studied. Two sn -1,3 specific lipases were used to catalyze this reaction: Lipozyme ® IM from Mucor miehei and lipase D from Rhizopus oryzae . The experimental results were acceptably fitted to
E. Molina, Belén Camacho, Luis Esteban, Alfonso Robles, Pedro A. González, Fernando Camacho   +5 more
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Phosphonate analogues of triacylglycerols are potent inhibitors of lipase

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1995
1,2-Dioctylcarbamoylglycero-3-O-p-nitrophenyl alkylphosphonates, with alkyl being methyl or octyl, were synthesised and tested as irreversible inhibitors of cutinase from Fusarium solani pisi and Staphylococcus hyicus lipase. Rapid inactivation of these enzymes occurred with a concomitant release of one mole of p-nitrophenol per mole of enzyme.
Hubertus M. Verheij, G.H. de Haas, M. L. M. Mannesse, J.-W.P. Boots, A.T. Slotboom, Maarten Robert Egmond, H. T. W. M. van der Hijden, R. Dijkman   +7 more
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Hydrolysis of emulsified mixtures of triacylglycerols by pancreatic lipase

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1999
Hydrolysis of the emulsified mixture of short-chain triacylglycerols by porcine pancreatic lipase in the presence of procolipase and micellar sodium taurodeoxycholate has been studied. Increase in the content of tributyrin and trioctanoin in the mixture with triacetin had highly cooperative effects on the formation of the interfacial lipase procolipase
Peeter Sikk, Tuuli Kaambre, Peeter Käämbre, Vello Tõugu, Heiki Vija   +4 more
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On the Similarity of Triacylglycerol and Acylcholesterol Lipases in Rat Brain

Journal of Neurochemistry, 1983
Abstract: Previously, we described a similar stimulating effect of adrenocorticotrophic hormone (ACTH) and ACTH‐related synthetic peptides on triacylglycerol (TAGL) and acylcholesterol (ACL) lipase activities of rat brain. In present study, TAGL and ACL activities from rat brain were further investigated and compared through the use of tri‐[3H ...
J. Boyer, O. Nobili, J. Arnaud
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Determination of triacylglycerol lipase activity using carbon‐13‐labeled triacylglycerols and nuclear magnetic resonance spectroscopy: Evidence that hepatic lipase hydrolyzes medium‐chain triacylglycerols [PDF]

Magnetic Resonance in Medicine, 1989
AbstractTriacylglycerol lipse activity was studied using glycerol [1‐13C] trioctanoate mixed with postheparin rat plasma. 13C NMR spectroscopy demonstrated triacylglycerol hydrolysis into free fatty acids with no difference at the 1,3 or 2 glycerol positions. There was no inhibition by high sodium concentration, consistent with lipase of hepatic origin.
Robert J. Dimand, Kenneth L. Cox, E. M. Bradbury   +2 more
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