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Functional binding analysis of human fibrinogen as an iron- and heme-binding protein

Koichi Orino1

  • 1Laboratory of Veterinary Biochemistry, School of Veterinary Medicine, Kitasato University, Towada City, Aomori, 034-8628, Japan, orino@vmas.kitasato-u.ac.jp.

Biometals : an International Journal on the Role of Metal Ions in Biology, Biochemistry, and Medicine
|July 19, 2013
PubMed

Human fibrinogen is a metal ion-binding protein, but its mechanism of binding with iron and heme has not been elucidated in detail. In this study, human fibrinogen was immobilized on CNBr-activated Sepharose 4B beads. The fibrinogen beads bound hemin (iron-protoporphyrin IX: PPIX) as well as iron ion released from ferrous ammonium sulfate (FAS) more efficiently than Sepharose 4B beads alone. Hemin bound to fibrinogen still exhibited pseudo-peroxidase activity. The affinity of fibrinogen binding to hemin, Sn-PPIX, Zn-PPIX and metal-free PPIX followed the order Sn-PPIX metal-free PPIX < hemin < Zn-PPIX; PPIX bound more non-specifically to control beads. FAS significantly enhanced the binding of hemin to fibrinogen beads. These results suggest that human fibrinogen directly recognizes iron ion, the PPIX ring and metal ions complexed with the PPIX ring, and that the binding of hemin is augmented by iron ions.

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