Studies of the ceruloplasmin-lactoferrin complex

Biochem Cell Biol. 2002;80(1):35-9. doi: 10.1139/o01-206.

Abstract

We have previously shown that iron-containing human lactoferrin (LF) purified from breast milk is able to form both in vitro and in vivo a complex with ceruloplasmin (CP), the copper-containing protein of human plasma. Here we present evidence that the CP-LF complex is dissociated by high concentrations of NaCl, CaCl2, or EDTA, or by decreasing the pH to 4.7. In addition, DNA, bacterial lipopolysaccharide, and heparin can displace CP from its complex with LF. Antibodies to either of the two proteins also cause dissociation of the complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calcium Chloride / pharmacology
  • Ceruloplasmin / metabolism*
  • Chromatography, Affinity
  • Chromatography, Gel
  • Edetic Acid / pharmacology
  • Electrophoresis, Polyacrylamide Gel
  • Humans
  • Hydrogen-Ion Concentration
  • Lactoferrin / metabolism*
  • Macromolecular Substances
  • Milk, Human / metabolism
  • Protein Binding / drug effects
  • Sodium Chloride / pharmacology

Substances

  • Macromolecular Substances
  • Sodium Chloride
  • Edetic Acid
  • Ceruloplasmin
  • Lactoferrin
  • Calcium Chloride