[Effect of the addition of hog pancreatic colipase on the permeability to glucose and the phase transition of phosphatidyl choline liposomes].

An interaction between porcine pancreatic coli-pase and lecithin liposomes is demonstrated by gel filtration assays. The extent of the colipase penetration into the phospholipid bilayer was assessed by permeability and calorimetry studies carried out on the liposome colipase complex. The addition of colipase to liposomes induces a three fold increase in the permeability to [6-H3] glucose. This result reflects a perturbation in the bilayer which may be the consequence of the colipase interaction. The phase transition temperature is not modified by the added colipase. This observation suggests that the perturbation brought by the protein does not affect the acyl chain packing of the bulk lipid. On the other hand the enthalpy of transition (delta H) is decreased from 8.9 to 7.8 kcal/mole by the addition of colipase to the lipid. This could be explained by the interaction of the colipase with neighbouring acyl chains which do not participate in the cooperative melting of the bulk lipid. In agreement with previous spectrophotometric observations, the present results are indicative of hydrophobic interactions between colipase and bilayer hydrocarbon chains.