Author/Authors :
Zakharova، نويسنده , , Elena T. and Shavlovski، نويسنده , , Mikhail M. and Bass، نويسنده , , Mikhail G. and Gridasova، نويسنده , , Anastasia A. and Pulina، نويسنده , , Maria O. and De Filippis، نويسنده , , Vincenzo and Beltramini، نويسنده , , Mariano and Di Muro، نويسنده , , Paolo and Salvato، نويسنده , , Benedetto and Fontana، نويسنده , , Angelo and Vasilyev، نويسنده , , Vadim B. and Gaitskhoki، نويسنده , , Vladimir S.، نويسنده ,
Abstract :
When added to human blood serum, the iron-binding protein lactoferrin (LF) purified from breast milk interacts with ceruloplasmin (CP), a copper-containing oxidase. Selective binding of LF to CP is evidenced by the results of polyacrylamide gel electrophoresis, immunodiffusion, gel filtration, and affinity 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 interacting with its counterpart. Kd for the CP/LF complex was estimated from Scatchard plot as 1.8 × 10−6 M. The CP/LF complex is found in various fluids of the human body. Upon injection into rat of human LF, the latter is soon revealed within the CP/LF complex of the blood plasma, from where the human protein is substantially cleared within 5 h.
Keywords :
lactoferrin , Ceruloplasmin , Ferroxidase , metalloproteins
