References: Lecithin
J Parenter Sci Technol. 1992 Jul-Aug;46(4):130-4.
A comparison of two commercially irradiated Trypticase Soy Agars containing lecithin and polysorbate 80.
Marsik F, Fowler J.
Becton Dickinson Microbiology Systems, Cockeysville, Maryland.
Gamma-radiation sterilized Trypticase Soy Agar containing lecithin and polysorbate 80 (TSA++) (Becton Dickinson Microbiology Systems, Cockeysville, MD) and irradiated TSA++ (Adams Scientific, West Warwick, RI) were tested by a quantitative spread plate method. Four bacteria Bacillus subtilis ATCC 6633, Pseudomonas aeruginosa ATCC 10145, Staphylococcus aureus ATCC 25923, Streptococcus pyogenes ATCC 19615 and the yeast Candida albicans ATCC 10231 were tested in two separate experiments using different lots of media. A strain of Aspergillus niger ATCC 16404, was tested by a qualitative streak plate method. The Becton Dickinson Microbiology Systems (BDMS) irradiated TSA++ overall recovered a greater number of organisms than the Adams Scientific TSA++ in both experiments and allowed for the earlier recovery of S. pyogenes ATCC 19615. The growth of A. niger ATCC 16404, was comparable on both media. Efficacy of the media to neutralize 1, 2 and 3% phenol as well as 0.001, 0.01 and 0.1% benzalkonium chloride (BC) solutions was done by a disk diffusion method using 2 gram-positive and 4 gram-negative bacteria. Both media showed complete neutralization of the 0.001 and 0.01% BC solutions and partial neutralization of the 0.1% BC solution. The BDMS TSA++ showed better neutralization of the 2 and 3% phenol solutions than the Adams Scientific TSA++. This data indicates that not all irradiated TSA++ media perform in an equivalent manner.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1453282&dopt=Abstract lecithin
Arterioscler Thromb. 1992 Jun;12(6):682-90.
A DNA polymorphism for LCAT is associated with altered LCAT activity and high density lipoprotein size distributions in baboons.
Rainwater DL, Blangero J, Hixson JE, Birnbaum S, Mott GE, VandeBerg JL.
Department of Genetics, Southwest Foundation for Biomedical Research, San Antonio, TX 78228-0147.
A polymorphic Pvu II site was mapped to intron 5 of LCAT, the gene encoding baboon lecithin: cholesterol acyltransferase (LCAT). In a study of 83 baboons, heterozygous baboons (Pv1/Pv2) had significantly higher LCAT enzyme activity levels than did baboons homozygous for the more common allele (Pv1/Pv1). LCAT genotype explained 6% of the total variation in LCAT enzyme activity. To test for allelic effects on cholesterol metabolism, we compared serum concentrations of high density lipoprotein (HDL) cholesterol and apolipoprotein A-I (apo A-I). We also compared distributions of cholesterol and apo A-I among three HDL size classes (HDL1, HDL2, and HDL3). All measurements were obtained for each baboon after long-term feeding of a basal diet low in cholesterol and fat and again after 7 weeks on an atherogenic diet. Heterozygous baboons had significantly lower serum levels of total cholesterol than did homozygotes. In addition, we detected significant effects of LCAT genotype on size distributions of HDL cholesterol and apo A-I on both diets but did not detect any genotype-by-diet interaction. Heterozygotes had increased amounts of cholesterol and apo A-I in HDL3 particles and lower amounts of cholesterol and apo A-I in the larger HDL size classes by comparison with homozygotes. Overall, the LCAT polymorphism explained a significant proportion of total variation in cholesterol (4-10%) and apo A-I (13%) distributions on both diets. Thus, the results indicate that the LCAT polymorphism is associated with significant differences in LCAT enzyme activity and with alterations in HDL compositions.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=1350465&dopt=Abstract lecithin
Gen Physiol Biophys. 1994 Oct;13(5):393-403.
The effect of albumin on incorporation of merocyanine 540 into phospholipid liposomes.
Sikurova L, Frankova R.
Department of Biophysics, Comenius University, Bratislava, Slovakia.
Absorption and fluorescence emission spectroscopy was applied to study the changes in albumin modified incorporation of merocyanine 540 into liposomes composed of different lecithins (DMPC, DPPC, POPC, and egg PC). Our results confirmed high affinity of merocyanine molecules toward albumin and revealed that albumin competed with all phospholipids used for binding merocyanine 540 molecules. However, the extent of this competition was determined by the kind of phospholipid. Albumin competed very successfully with lecithins containing saturated fatty acid chains (DPPC, DMPC) and weakly with unsaturated lecithins (POPC, egg PC) for binding merocyanine 540 molecules.
Laxative online source: www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=7797047&dopt=Abstract lecithin
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