References: Lecithin
Chem Phys Lipids. 1994 Jan;69(1):87-94.
Autoxidation and antioxidant activity of ubiquinol homologues in large unilamellar vesicles.
Cipollone M, Fiorentini D, Galli MC, Sechi AM, Landi L.
Dipartimento di Biochimica G. Moruzzi, Universita degli Studi di Bologna, Italy.
The antioxidant activity of ubiquinol homologues with different side-chain length such as ubiquinol-3 and ubiquinol-7 was compared with that of alpha-tocopherol when peroxidation was induced by the water-soluble initiator 2,2'-azobis-(2-amidinopropane hydrochloride). In large unilamellar vesicles containing equal amounts of alpha-tocopherol, ubiquinol-3 and ubiquinol-7 the rates of inhibition were very similar but the stoichiometric factor of quinols was approximately 1. To explain this low value, which is one-half of that found when the autoxidation was performed in apolar solvents (Chem. Phys. Lipids (1992) 61, 121-130), the oxidation of alpha-tocopherol and ubiquinol-3 initiated by the azocompound was studied both in methanol and in dimiristoyl-lecithin vesicles. The results obtained show that the ubiquinol homologues undergo a radical chain reaction taking place at the polar interface and suggest that the average preferred location of both quinol headgroups is near to the outer surface of the bilayer.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8200059&dopt=Abstract lecithin
FEBS Lett. 1992 Nov 23;313(2):169-72.
Ca(2+)-mediated interaction between negatively charged and neutral liposomes.
Budker VG, Kiseleva HV, Serebryakova MV, Sokoloff AV.
Institute of Bioorganic Chemistry, Siberian Division of the Russian Academy of Sciences, Novosibirsk.
In the present work it is shown that large unilamellar lecithin/cholesterol liposomes are able to sequester small negatively charged liposomes in the presence of divalent cations. Evidence is presented suggesting that the sequestration occurs via the formation of membrane invaginations transformed further into intraliposomal vesicles.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1426285&dopt=Abstract lecithin
Biochem Biophys Res Commun. 1997 Mar 27;232(3):783-7.
Identification of a domain of lecithin-cholesterol acyltransferase that is involved in interfacial recognition.
Adimoolam S, Jonas A.
Department of Biochemistry, University of Illinois, College of Medicine at Urbana-Champaign 61801, USA.
Lecithin-cholesterol acyltransferase (LCAT) is an interfacial enzyme that acts on lipid substrates on the surface of high density lipoproteins (HDL). Based on observations with other interfacial lipases, we propose that LCAT contains a surface region of 25 amino acids linked by a disulfide bond (C50-C74) that is involved in the binding of LCAT to lipoproteins. Using LCAT cDNA, we have deleted most of this region (delta 53-71) and expressed the mutant enzyme (LCAT delta 53-71) in COS-1 cells. The deletion mutant is expressed and secreted at levels similar to wildtype LCAT, suggesting that the deleted region is located on the surface of the enzyme and is not required for folding. The enzymatic activity of the mutant was tested using two interfacial substrates, reconstituted HDL (rHDL) and low density lipoprotein (LDL), as well as a water soluble substrate, p-nitrophenyl butyrate (PNPB). There was no reaction with rHDL and LDL, but 30% of the activity with PNPB was retained. This suggests that the deleted region plays a role in interfacial binding, while the active site core is not disrupted. We thus conclude that this region (C50-C74) forms part of the interfacial binding domain of LCAT.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=9126354&dopt=Abstract lecithin
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