Results 171 to 180 of about 48,866 (213)
Some of the next articles are maybe not open access.
Regulation of lipoprotein lipase by Angptl4
Trends in Endocrinology & Metabolism, 2014Triglyceride (TG)-rich chylomicrons and very low density lipoproteins (VLDL) distribute fatty acids (FA) to various tissues by interacting with the enzyme lipoprotein lipase (LPL). The protein angiopoietin-like 4 (Angptl4) is under sensitive transcriptional control by FA and the FA-activated peroxisome proliferator activated receptors (PPARs), and its ...
Dijk, W., Kersten, A.H.
openaire +3 more sources
Lipoprotein lipase in diabetes
Diabetes/Metabolism Reviews, 1987Lipoprotein lipase has a central role in the metabolism of both triglyceride-rich particles and high density lipoproteins, and it is one determinant of both serum triglyceride and HDL concentrations. In man the enzyme activity in both adipose tissue and skeletal muscle is insulin dependent, and therefore it varies in diabetes according to ambient ...
openaire +2 more sources
1976
The degradation of triglyceride-rich plasma lipoproteins and the uptakeof their lipid constituents by tissues is dependent on enzymaticactivities which reside on or near the luminal surface of the capillary endothelium. Intravenous heparin injection releases a group of lipid hydrolyzing activities that are not normally present in plasma.
W. V. Brown +4 more
openaire +1 more source
The degradation of triglyceride-rich plasma lipoproteins and the uptakeof their lipid constituents by tissues is dependent on enzymaticactivities which reside on or near the luminal surface of the capillary endothelium. Intravenous heparin injection releases a group of lipid hydrolyzing activities that are not normally present in plasma.
W. V. Brown +4 more
openaire +1 more source
The effect of lipoprotein lipase and hepatic lipase on the electrophoretic mobility of lipoprotein-X
Clinica Chimica Acta, 1978Lipoprotein-X containing plasma from a patient with familial lecithin:cholesterol acyltransferase (LCAT) deficiency, was used as substrate and incubated with postheparin plasma or partly purified lipases. LP-X could not be demonstrated by agar gel electrophoresis after incubation with postheparin plasma from a healthy subject, from a patient with ...
J, Sauar, S, Ritland, R, Holme, R, Horn
openaire +2 more sources
Binding of deoxycholate to lipoprotein lipase
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1979Abstract Binding of deoxycholate to lipoprotein lipase from bovine milk was demonstrated by equilibrium dialysis and by charge shift electrophoresis. The detergent increased the solubility and stability of the enzyme in aqueous buffers, but did not change its elution position on gel filtration.
G, Bengtsson, T, Olivecrona
openaire +2 more sources
Interaction of Lipoprotein Lipase with Heparina
Annals of the New York Academy of Sciences, 1989The hydrolysis of triglyceride-rich plasma lipoproteins is initiated by lipoprotein lipase (LPL) located at the luminal surface of endothelial cells. We previously reported that LPL binds to cultured endothelial cells with a Km of 2.7 x 10(-7) M and that this binding is inhibited by heparinase, heparin, or heparan sulfate.
K, Oka +3 more
openaire +2 more sources
Lipaemia in lipoprotein lipase deficiency
Journal of Paediatrics and Child Health, 2016See ...
Anthony, Liu +2 more
openaire +2 more sources
Atherosclerosis, 1975
Rat heart lipoprotein lipase was highly purified by affinity chromatography using heparin-Sepharose 4B. When extracts of acetone powder were applied to columns, lipase activity was firmly bound to the gel matrix and was later eluted with 1.5 M NaCl. At this stage the eluted enzyme was purified 1500-fold.
J S, Twu, A S, Garfinkel, M C, Schotz
openaire +2 more sources
Rat heart lipoprotein lipase was highly purified by affinity chromatography using heparin-Sepharose 4B. When extracts of acetone powder were applied to columns, lipase activity was firmly bound to the gel matrix and was later eluted with 1.5 M NaCl. At this stage the eluted enzyme was purified 1500-fold.
J S, Twu, A S, Garfinkel, M C, Schotz
openaire +2 more sources
Physiological regulation of lipoprotein lipase
Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids, 2014The enzyme lipoprotein lipase (LPL), originally identified as the clearing factor lipase, hydrolyzes triglycerides present in the triglyceride-rich lipoproteins VLDL and chylomicrons. LPL is primarily expressed in tissues that oxidize or store fatty acids in large quantities such as the heart, skeletal muscle, brown adipose tissue and white adipose ...
openaire +3 more sources

