Abstract
The interaction between a soluble protein α-lactalbumin (α-LA) and dimyristoyl phosphatidylcholine (DMPC) liposomes was studied using an ultrasonic technique. The ultrasonic properties of DMPC liposomes changed significantly after the addition of α-LA at pH 3. The lipid bilayer transition temperature became higher and transition anomalies of DMPC liposomes were enhanced in the presence of α-LA under these conditions. At the same time, the size of the liposomes apparently decreased as revealed by the clearing of suspensions.
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