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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)

Abstract

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

Keywords

Small Vesicle Complex Particle Liposome Preparation Small Unilamellar Vesicle Large Unilamellar Vesicle 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

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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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