Ceruloplasmin and myeloperoxidase in complex affect the enzymatic properties of each other.

@article{Sokolov2008CeruloplasminAM,
  title={Ceruloplasmin and myeloperoxidase in complex affect the enzymatic properties of each other.},
  author={Alexey V Sokolov and Kira V. Ageeva and Maria O. Pulina and Olga S Cherkalina and Valeria R. Samygina and Irina I. Vlasova and Oleg M. Panasenko and Elena T. Zakharova and Vadim B. Vasilyev},
  journal={Free radical research},
  year={2008},
  volume={42 11-12},
  pages={989-98}
}
Ceruloplasmin (CP), the multicopper oxidase of plasma, interacts with myeloperoxidase (MPO), an enzyme of leukocytes, and inhibits its peroxidase and chlorinating activity. Studies on the enzymatic properties shows that CP behaves as a competitive inhibitor impeding the binding of aromatic substrates to the active centre of MPO. The contact between CP and MPO probably entails conformational changes close to the p-phenylenediamine binding site in CP, which explains the observed activation by MPO… CONTINUE READING