References: Lecithin
Lipids. 2003 Sep;38(9):947-56.
Solubilization of carotenoids from carrot juice and spinach in lipid phases: II. Modeling the duodenal environment.
Rich GT, Faulks RM, Wickham MS, Fillery-Travis A.
Institute of Food Research, Norwich Research Park, Colney, Norwich, United Kingdom NR4 7UA.
We have been investigating the factors determining the bioavailability of carotenoids from vegetables. The previous paper [Rich, G.T., Bailey, A.L., Faulks, R.M., Parker, M.L., Wickham, M.S.J., and Fillery-Travis, A. (2003) Solubilization of Carotenoids from Carrot Juice and Spinach in Lipid Phases: I. Modeling the Gastric Lumen, Lipids 38, 933-945] modeled the gastric lumen and studied the solubilization pathway of carotenes and lutein from carrot juice and homogenized spinach to oil. Using the same vegetable preparations, we have extended our investigations to solubilization pathways potentially available in the duodenum and looked at the ease of solubilization of carotenes and lutein within simplified lipid micellar and oil phases present within the duodenum during digestion. Micellar solubility of raw spinach carotenoids was low and was enhanced by freezing, which involved a blanching step. The efficiency of solubilization of carotenoids in glycodeoxycholate micelles decreased in the order lutein(carrot) > lutein(blanched-frozen spinach) > carotene(blanched-frozen spinach) > carotene(carrot). Frozen spinach carotenoids were less soluble in simple micelles of taurocholate than of glycodeoxycholate. The results comparing the solubility of the carotenoids in mixed micelles (bile salt with lecithin) with simple bile salt micelles are explained by the relative stability of the carotenoid in the organelle compared to that in the micelle. The latter is largely determined by the polarity of the micelle. Below their critical micelle concentration (CMC), bile salts inhibit transfer of carotenoids from tissue to a lipid oil phase. Above their CMC, the bile salts that solubilize a carotenoid can p
Proc Soc Exp Biol Med. 1988 Nov;189(2):196-200.
A nonimmunoglobulin precipitin to tissue extracts in pathological human sera.
Kim DS, Milgrom F.
Department of Microbiology, School of Medicine, State University of New York, Buffalo 14214.
An alpha-globulin component was noted in pathological human sera, which produced gel precipitation reactions with extracts of human and animal liver. The highest incidence of the precipitin was found in malaria (95%), renal graft rejection (81%), and rheumatoid arthritis (57%). The precipitinogen was thermostable and ethanol soluble; of two precipitation lines formed by this component, one merged into identity reaction with a line produced by commercial lecithin of bovine origin. The possible diagnostic application of the reactions noted was considered.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2461571&dopt=Abstract lecithin
Biochemistry. 2003 Nov 11;42(44):12805-12. ["Gene","window.top.location='Laxative online source: www.ncbi.nlm.nih.gov:80/entrez/query.fcgi?db=PubMed&cmd=Display&dopt=pubmed_gene&from_uid=14596594'","",""],
Lecithin retinol acyltransferase is a founder member of a novel family of enzymes.
Jahng WJ, Xue L, Rando RR.
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 45 Shattuck Street, Boston, Massachusetts 02115, USA.
Lecithin retinol acyltransferase (LRAT) catalyzes the reversible esterification of vitamin A using lecithin as the acyl donor. LRAT is the founder member of a new class of enzymes, which include class II tumor suppressors, proteins essential for development, and putative proteases. All of these proteins possess Cys and His residues homologous to C161 and H60 of LRAT. These two residues are shown here to be essential for LRAT activity and are part of a catalytic dyad reminiscent of that found in thiol proteases. However, the local primary sequence contexts of C161 and H60 of LRAT and family are not at all homologous to those found in the approximately 20 thiol protease families. Moreover, LRAT shows pKs of 8.3 and 10.8, compared to approximately 4.0 and 8.5 observed in the thiol proteases. LRAT also contains Gln177 and Asp67 residues, which are largely conserved in the homologues. However, neither of these residues is essential for catalysis. Thiol proteases often contain catalytically essential Asp or Gln residues. It is concluded that LRAT is the founder member of a new class of Cys-His enzymes with diverse functions.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=14596594&dopt=Abstract lecithin
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