References: Lecithin
Biochem J. 1995 Sep 15;310 ( Pt 3):989-95.
Solubilization and separation of two distinct carnitine acyltransferases from hepatic microsomes: characterization of the malonyl-CoA-sensitive enzyme.
Broadway NM, Saggerson ED.
Department of Biochemistry and Molecular Biology, University College London, U.K.
Conditions have been developed for the solubilization of hepatic microsomal carnitine acyltransferase activity in good yield, with excellent long-term stability and with retention of malonyl-CoA sensitivity. Solubilized microsomal carnitine acyltransferase activity can be separated into malonyl-CoA-sensitive and -insensitive activities either by gel filtration on Superdex 200 or by anion-exchange chromatography on Resource Q. On gel filtration the apparent molecular masses of the malonyl-CoA-sensitive and -insensitive activities are approx. 300 kDa and 60 kDa respectively. The malonyl-CoA-sensitive and -insensitive activities have different fatty-acyl-chain-length specificities and different stabilities in the detergent octyl glucoside. Together these findings indicate that the malonyl-CoA-sensitive and -insensitive activities are due to different enzymes. The malonyl-CoA sensitivity of the inhibitable enzyme is markedly increased on reconstitution into soybean L-alpha-lecithin liposomes, demonstrating that phospholipids play a crucial role in the inhibition by this metabolite. Evidence is also provided that the malonyl-CoA-sensitive microsomal carnitine acyltransferase is a different enzyme from the malonyl-CoA-sensitive carnitine palmitoyltransferase found in the mitochondrial outer membrane. The possible physiological role of the two microsomal acyltransferases is discussed.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=7575437&dopt=Abstract lecithin
Horm Metab Res. 1992 Jun;24(6):289-96.
Effects of probucol on plasma lipids, lipoproteins and parameters of high density lipoprotein metabolism.
Wetterau JR, Combs KA, Albers HW, Lamkin G, Stein EA, Barnhart RL, Chi EM, Jackson RL, Harmony JA.
Department of Pharmacology and Cell Biophysics, University of Cincinnati.
Eight patients with primary hypercholesterolemia were treated with probucol for 17 weeks. Plasma total cholesterol, low density lipoprotein (LDL)-cholesterol, and high density lipoprotein (HDL)-cholesterol decreased by 16.6, 15.0 and 25.7%, respectively, in response to probucol treatment. Plasma levels of apolipoprotein B and apolipoprotein A-I also decreased, while apolipoprotein A-II concentrations were unchanged. The decrease in HDL-cholesterol levels was associated with a reduction in HDL particle size. No changes in the plasma lecithin:cholesterol acyltransferase activity or mass occurred in response to probucol treatment. In contrast, a significant 25% increase in plasma cholesteryl ester and triglyceride transfer activity occurred following probucol treatment. There was a positive correlation (R = 0.94) between cholesterol ester and triglyceride transfer. We propose that the increase in lipid transfer activity may in part explain the changes in HDL concentration and size, as well as the previously reported effect probucol has on reducing atherosclerosis in animal models.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1634195&dopt=Abstract lecithin
Pharmacol Res. 1997 Aug;36(2):135-9.
High rate of intestinal absorption of the phospholipid anlaogue 1-dodecyl 2-[1-14C] octanamido-sn-2-deoxy-glycero-3-phosphocholine in the rat.
Boucrot P, Bourass J, Elkihel L, Letourneux Y, Gandemer G.
Laboratoire d'Etude des Interactions des Molecules Alimentaires, I. N.R.A. BP7 1627, 44316 Nantes Cedex 3, France.
The phospholipid analogue with two short fatty chains, 1-dodecyl-2-[1-14C] octanamido-sn-2-deoxy-glycero-3-phosphocholine ([14C] phospholipid analogue), with a non-hydrolyzable bond at position 2 of the glycerol, is an inhibitor of phospholipase A2. It was obtained after chemical synthesis and 0.5 micromol was solubilized in Na+ taurocholate with an equimolar amount of 1-octadecanoyl 2-[3H]eicosatetraenoyl-sn- glycero-3-phosphocholine which is the current substrate of phospholipases A2. Both molecules were introduced into the duodenum of rats in order to follow their captations by intestinal mucosa cells for 30, 60 or 90 min. The [14C] phospholipid analogue was poorly split by phospholipases A2 (pancreatic juice and intracellular enzymes). It disappeared from the intestinal contents (87% of the dose gone in 90 min) as rapidly as the tritiated lecithin (81%) but this was later split by the phospholipases at a higher rate. Copyright 1997 The Italian Pharmacological Society.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9344642&dopt=Abstract lecithin
Lecithin online literature
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