Enthalpy State of Different Liposome Preparations of Dimyristoyl Phosphatidylcholine and Their Stability in the Presence of a Complex Forming Protein

  • Ignace Hanssens
  • Willy Herreman
  • Jean-Claude Van Ceunebroeck
  • Frans Van Cauwelaert
Part of the NATO Advanced Science Institutes Series book series (NSSA, volume 71)


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


Small Vesicle Complex Particle Liposome Preparation Small Unilamellar Vesicle Large Unilamellar Vesicle 
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Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • Ignace Hanssens
    • 1
  • Willy Herreman
    • 1
  • Jean-Claude Van Ceunebroeck
    • 1
  • Frans Van Cauwelaert
    • 1
  1. 1.Interdisciplinair Research CentrumKatholieke Universiteit LeuvenKortrijkBelgium

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