Results 51 to 60 of about 26,185 (255)

Lipid transfer from insect fat body to lipophorin: comparison between a mosquito triacylglycerol-rich lipophorin and a sphinx moth diacylglycerol-rich lipophorin

Journal of Lipid Research, 1996
Two insect lipoproteins, triacylglycerol-rich Aedes aegypti lipophorin and diacylglycerol-rich Manduca sexta lipophorin, were compared in their ability to load neutral lipid from fat body. When fat body of M.
J E Pennington, R H Nussenzveig, M C Van Heusden   +2 more
doaj   +1 more source

Arylacetamide deacetylase attenuates fatty-acid-induced triacylglycerol accumulation in rat hepatoma cells

Journal of Lipid Research, 2010
Mobilization of hepatic triacylglycerol stores provides substrates for mitochondrial β-oxidation and assembly of VLDLs; however, the identity of lipolytic enzymes involved in the regulation of this process remains largely unknown.
Vivien Lo, Bruce Erickson, Michaela Thomason-Hughes, Kerry W.S. Ko, Vernon W. Dolinsky, Randy Nelson, Richard Lehner   +6 more
doaj   +1 more source

Liver and extrahepatic contributions to postheparin serum lipase activity of the rat [PDF]

, 1974
The influence of the amount of heparin injected on the contributions of liver and of extrahepatic tissues to the lipase activity of postheparin serum of the rat was studied.
Hülsmann, W.C. (William), Jansen, H. (Hans)   +1 more
core   +1 more source

Effect of increasing lipid loads on the ability of the endoplasmic reticulum to transport lipid to the Golgi

Journal of Lipid Research, 2000
We have previously shown (Mansbach, C. M. and P. J. Nevin, 1998. J. Lipid Res. 39: 963–968) that after the development of a mass steady state with respect to triacylglycerol absorption in rats, the introduction of radiolabeled trioleoylglycerol, while ...
C.M. Mansbach, R. Dowell
doaj   +1 more source

Crystal structure of Pseudomonas aeruginosa lipase in the open conformation - The prototype for family I.1 of bacterial lipases [PDF]

, 2000
The x-ray structure of the lipase from Pseudomonas aeruginosa PAO1 has been determined at 2.54 Angstrom resolution. It is the first structure of a member of homology family I.1 of bacterial lipases.
Dijkstra, BM, Jaeger, KE, Lang, DA, Liebeton, K, Nardini, M   +4 more
core   +1 more source

Efficient Phagocytosis Requires Triacylglycerol Hydrolysis by Adipose Triglyceride Lipase [PDF]

Journal of Biological Chemistry, 2010
Macrophage phagocytosis is an essential biological process in host defense and requires large amounts of energy. To date, glucose is believed to represent the prime substrate for ATP production in macrophages. To investigate the relative contribution of free fatty acids (FFAs) in this process, we determined the phagocytosis rates in normal mouse ...
Chandak, Prakash G., Radović, Branislav, Aflaki, Elma, Kolb, Dagmar, Buchebner, Marlene, Fröhlich, Eleonore, Magnes, Christoph, Sinner, Frank, Haemmerle, Guenter, Zechner, Rudolf, Tabas, Ira, Levak-Frank, Sanja, Kratky, Dagmar   +12 more
openaire   +2 more sources

Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity despite close relationship to acyl protein thioesterases

Journal of Lipid Research, 2012
Sequence homology indicates the existence of three human cytosolic acyl protein thioesterases, including APT1 that is known to depalmitoylate H- and N-Ras. One of them is the lysophospholipase-like 1 (LYPLAL1) protein that on the one hand is predicted to
Marco Bürger, Tobias J. Zimmermann, Yasumitsu Kondoh, Patricia Stege, Nobumoto Watanabe, Hiroyuki Osada, Herbert Waldmann, Ingrid R. Vetter   +7 more
doaj   +1 more source

Ultrasound-assisted biosynthesis of novel methotrexate-conjugates [PDF]

, 2018
New methotrexate-acylglycerols and methotrexate-cyclodextrins (, and -CD) conjugates were obtained via esterification or transesterification reactions.
Cavaco-Paulo, Artur, Noro, Jennifer Martins, Reis, R. L., Silva, Carla   +3 more
core   +1 more source

ISOLATION AND PURIFICATION OF LIPASE FROM COCOA BEANS (Theobroma cacao. L.) OF CLONE PBC 159

Indonesian Journal of Chemistry, 2010
Lipase (triacylglycerol acylhydrolase, EC 3.1.1.3) was extracted and purified from acetone dry powder of cocoa (Theobroma cacao. L.) of clone PBC 159 extract.
Ratna Agung Samsumaharto
doaj   +1 more source

Impact of lipoprotein lipase gene polymorphism, S447X, on postprandial triacylglycerol and glucose response to sequential meal ingestion [PDF]

, 2016
Lipoprotein lipase (LPL) is a key rate-limiting enzyme for the hydrolysis of triacylglycerol (TAG) in chylomicrons and very low-density lipoprotein. Given that postprandial assessment of lipoprotein metabolism may provide a more physiological perspective
Anne-Marie Minihane, Christine Williams, Goldberg, Israa Shatwan, Julie Lovegrove, Karani Vimaleswaran, Kim Jackson, Kozaki   +7 more
core   +2 more sources