Ca2+ binding to bovine lactoferrin enhances protein stability and influences the release of bacterial lipopolysaccharide.

@article{Rossi2002Ca2BT,
  title={Ca2+ binding to bovine lactoferrin enhances protein stability and influences the release of bacterial lipopolysaccharide.},
  author={Paola Rossi and Francesco Giansanti and Alberto Boffi and Maria Ajello and Piera Valenti and Emilia Chiancone and Giovanni Antonini},
  journal={Biochemistry and cell biology = Biochimie et biologie cellulaire},
  year={2002},
  volume={80 1},
  pages={41-8}
}
Bovine lactoferrin (bLf) is known to damage the outer membrane of Gram-negative bacteria by binding to bacterial lipopolysaccharide (LPS). We report that LPS is released from bacterial outer membranes also when apo- or metal-saturated Lf is separated from bacterial cells by a dialysis membrane. This process occurs in phosphate-buffered saline with no added Ca2+ and Mg2+ and is hindered by addition of these cations. The effect of bLf is similar to that induced by EDTA and has been ascribed to… CONTINUE READING

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