References: Lecithin
J Lipid Res. 1967 Jan;8(1):46-53.
Post-heparin serum lecithinase in man and its positional specificity.
Vogel WC, Bierman EL.
Medical Service, Veterans Administration Hospital and Department of Medicine, University of Washington School of Medicine, Seattle, USA.
Lecithinase activity in post-heparin serum has been demonstrated. Phosphatidyl choline (PC) can be degraded to lysophosphatidyl choline and fatty acids at a rate of more than 1 micromole/hr per ml of serum in an incubation system containing PC, 0.1 M glycine-NaOH buffer (pH 9.6), and deoxycholate. This activity cannot be found in serum obtained prior to the injection of heparin. Post-heparin serum lecithinase can be distinguished from the heat-stable pancreatic lecithinase by the markedly different effects of heat, paraoxon, and EDTA, and from serum lecithin:cholesterol acyltransferase by the differential effect of p-hydroxymercuribenzoate. In contrast to the acyltransferase and to pancreatic lecithinase, which are active at the beta (C-2) position of lecithin, post-heparin serum lecithinase is active at alpha' (C-1) position.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=14564704&dopt=Abstract lecithin
J Lipid Res. 1967 Mar;8(2):155-8.
Reversed-phase partition thin-layer chromatography of rat liver lecithins to yield eight simple phosphatidyl cholines.
Arvidson GA.
Department of Physiological Chemistry, University of Lund, Lund, Sweden.
The four fractions obtained by argentation thin-layer chromatography of intact rat liver lecithins can be further subdivided by reversed-phase partition thin-layer chromatography on hydrophobic kieselguhr. The resultant eight fractions contain virtually only one saturated and one unsaturated acid each.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=14564726&dopt=Abstract lecithin
Protein Eng. 1995 Nov;8(11):1129-35.
Essential dynamics of the cellular retinol-binding protein--evidence for ligand-induced conformational changes.
van Aalten DM, Findlay JB, Amadei A, Berendsen HJ.
Department of Biochemistry and Molecular Biology, University of Leeds, UK.
The cellular retinol-binding protein (CRBP) is an intracellular retinol carrier protein belonging to a family of hydrophobic ligand-binding proteins. It transports retinol to specific locations in the cell where, for instance, it is esterified for storage. Recently solved crystallographic structures of CRBP homologues with and without bound ligand do not provide evidence for a ligand-induced conformational change. However, it has been shown that there is a difference in binding of holo-CRBP and apo-CRBP to lecithin-retinol acyltransferase. Moreover, proteolysis of holo-CRBP and apo-CRBP yields different products, indicating a difference in structure or dynamics between the two forms. Here, we present the results of molecular dynamics simulations of holo-CRBP and apo-CRBP. The simulations show a significant difference in conformation, in agreement with experimental results. The essential dynamics method was used to study differences in dynamics between the apo and holo forms of CRBP, and showed inhibition of essential motions upon ligand binding. It also revealed large correlated motions of retinol with regions of the protein, pointing to a possible retinol entry/exit site.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8819978&dopt=Abstract lecithin
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