Interaction of lactoferrin with ceruloplasmin

When added to human blood serum, the iron-binding protein lactoferrin (LF) purified from breast milk interacts with ceruloplasmin (CP), a copper-conta ining oxidase. Selective binding of LF to CP is evidenced by the results of polyacrylamide gel electrophoresis, immunodiffusion, gel filtration, and a ffinity chromatography. The molar stoichiometry of CP:LF in the complex is 1:2. Near-uv circular dichroism spectra of the complex showed that neither of the two proteins undergoes major structural perturbations when interacti ng with its counterpart, K-d for the CP/LF complex was estimated from Scatc hard plot as 1.8 x 10(-6) M. The CP/LF complex is found in various fluids o f the human body. Upon injection into rat of human LF, the latter is soon r evealed within the CP/LF complex of the blood plasma, from where the human protein is substantially cleared within 5 h. (C) 2000 Academic Press.