Enthalpy State of Different Liposome Preparations of Dimyristoyl Phosphatidylcholine and Their Stability in the Presence of a Complex Forming Protein
Bovine α-lactalbumin was used to study the influence of the protein conformation on its interaction with phosphatidylcholine liposomes. The isoionic point of α-lactalbumin is at pH 5, and it has been demonstrated that between pH 4 and 2, the protein undergoes a conformational change with a concomittant increase in α-helicity.1 The α-helices in α-lactalbumin are amphipatic in the same way as in apolipoproteins.2
KeywordsSmall Vesicle Complex Particle Liposome Preparation Small Unilamellar Vesicle Large Unilamellar Vesicle
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