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At least 145 records · Page 8Linked to original sources
PubMed1993

Fatty acid composition of human milk triglyceride species. Possible consequences for optimal structures of infant formula triglycerides.

Human milk triglycerides (TGs) were separated into 14 fractions by silver ion high-performance liquid chromatography (HPLC) with light-scattering detection (LSD). Subsequent fractionation by reversed-phase HPLC-LSD resulted in 75 subfractions. The major 48 were analysed by gas chromatography for their intact TG and fatty acid (FA) compositions. Using a constrained non-linear optimization computer program, the FA compositions and abundances of 170 different TG combinations were calculated. The major two, 16:0/18:1/18:1 (11.8 mol%) and 16:0/18:1/18:2 (10.0 mol%), were almost twice as abundant as expected from random FA distribution. The apolarities of 16:0 and 18:0 seem to be modulated by unsaturated FAs (18:1, 18:2) or medium-chain FAs (MCFAs; 8:0-12:0). MCFAs were present in 19 mol%. Of these, 7.2 mol% are likely to harbour stereospecific structures with an MCFA at sn-3, 16:0 or 14:0 at sn-2, and 18:1 or 18:2 at sn-1. These structures are excellent substrates for lingual and gastric lipases, producing products that assist in duodenal TG lipolysis.

Chromatography, Gas↗
PubMed1989

Interaction of ApoA-1 and ApoE-3 with triglyceride-phospholipid emulsions containing increasing cholesterol concentrations. Model of triglyceride-rich nascent and remnant lipoproteins.

The cholesterol content of triglyceride-rich lipoproteins increases during their catabolism in circulation. We therefore studied the binding of the exchangeable apoprotein apoA-1 and apoE-3 to triolein-rich emulsions with increasing cholesterol content. Five emulsion systems containing 83.1-88.8% (w/w) triolein, 9.3-10.1% egg yolk phosphatidylcholine, and 1.1-7.3% cholesterol were isolated from sonicated lipid mixtures by flotation. Negative stain EM of emulsions containing 1.1 and 7.3% cholesterol showed polydisperse populations of large spherical particles with diameters of 106 +/- 39 and 108 +/- 57 nm. These values are similar to particle diameters calculated from the lipid composition data. No lamellar structures were observed by EM, even after addition of apoA-1 at a molar ratio to lecithin of 10(-2). Apolipoproteins apoA-1 and apoE-3 bound to the particles in a saturable manner without altering particle morphology. We found a dissociation constant Kd = 7.4 x 10(-7) M and a binding capacity N = 3.9 x 10(-3) proteins/lecithin for apoA-1 with particles containing 1.1% cholesterol; the Kd and N values for apoE-3 were very similar. When the emulsion particles were saturated with cholesterol at 7.3%, the protein binding capacity N sharply decreased to 0.6 x 10(-3) (apoA-1) and 0.7 x 10(-3) proteins/lecithin (apoE-3), but the Kd values were virtually unchanged. No change in N occurred when the particle cholesterol content was increased from 1.1 to 3.7%, which spans the normal physiological range. These results suggest that increases in lipoprotein cholesterol content above 3.7% may be responsible for impaired apoprotein redistribution and altered metabolism of remnants such as beta-VLDL.

Apolipoprotein A-I↗