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• W1824583883 abstract "Triolein particles stabilized by a phosphatidylcholine monolayer were used to study the lipoprotein lipase (LpL) reaction. They were prepared in two different sizes and with triolein and phosphatidylcholine in the molar ratios of 0.9–1.2: 1 (small particles) and 8–17: 1 (large particles). The rate of hydrolysis by LpL of phosphatidylcholine on the surface of both lipid particles was only 1/20 as much as that of triolein, even if it was activated to the maximum by apolipoprotein C-II (apoC-II). Thus, the phospholipase activity of LpL was low enough to measure the initial rate of hydrolysis of triolein without causing a gross change of the surface of the lipid particle. When the hydrolysis of triolein by LpL was monitored, fatty acid was released at a constant rate until all of the triolein molecules were hydrolyzed. The enzyme required 220±17 and 66±9nM apoC-II for its half-maximal activity (Km (apoC-II)) with small and large particles as a substrate (1.15 mM triolein for small and 2.13 mM triolein for large particles), respectively, using various concentrations of LpL. The Km(apoC-II) values for these two substrates became similar when LpL activity was analyzed with respect to the density of apoC-II on the phosphatidylcholine monolayer at the surface of the particles (bound apoC-II/phosphatidyl—choline). The concentration of substrate particles did not affect the Km(apoC-II) values. The presence of an adequate amount of apoC-II increased the maximal activity of LpL (Vmax(triolein)) from 0.48±0.21 to 6.81±0.45 and from 0.32±0.04 to 7.13±0.64 mmol/h/mg with a slight decrease in the apparent Michaelis constant (Km(triolein)) for small (from 90 to 54 μM triolein) and large (from 1.00 to 0.65 itim triolein) particles, respectively. Although the apparent Km for triolein in large particles was about ten times greater than that in small particles, the values became similar when they were corrected for the concentration of phosphatidylcholine (50–100 μM phosphatidylcholine), which corresponded to the surface area of the substrate particles. it was suggested that bound apoC-II molecules were transferred relatively slowly to other lipid particles while LpL molecules moved rapidly among the lipid particles. These results indicatde that i)LPL activity is modulated by the concentration of apoC-II which is bound to the surface of the substrate particles, ii) LpL attacks triolein in or near the phosphatidylcholine layer at the surface of lopid particles, and iii) apoC-II activates LpL by increasing the catalytic rate with little change in the affinity of triolein for the enzyme." @default.
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• W1824583883 date "1984-10-01" @default.
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• W1824583883 title "Mechanism of Action of Lipoprotein Lipase on Triolein Particles: Effect of Apolipoprotein C-II1" @default.
• W1824583883 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a135008" @default.
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