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- W2024005013 abstract "Multilamellar liposomes made of equimolar mixtures of dimyristoyl and distearoylphosphatidylcholine were hydrolysed by porcine pancreatic phospholipase A2. Ph-stat titration, equilibrium gel filtration and differential scanning calorimetry were used to study respectively the enzymic hydrolysis, the enzyme binding and the lipid phase repartition. We demonstrated that the optimal enzyme activity observed in the region where liquid crystalline and gel lipid phases coexist, is due to a drastic increase of the enzyme binding to its substrate. It is suggested that the border region separating the lipid phases could be a privileged site for enzyme insertion. Increase of lateral compressibility due to coexistence of solid and fluid lipid phases will promote the penetration of the hydrophobic interface recognition site (IRS) of phospholipase A2 into the lipid matrix whereas the active site, distinct from the IRS will attack its substrate independently of the lipid physical state." @default.
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- W2024005013 date "1981-08-01" @default.
- W2024005013 modified "2023-09-27" @default.
- W2024005013 title "Lipid phase separation mediates binding of porcine pancreatic phospholipase A2 to its substrate" @default.
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- W2024005013 doi "https://doi.org/10.1016/0006-291x(81)91604-1" @default.
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