Binding Analysis of Human Immunoglobulin G as a Zinc-Binding Protein

• Main Authors: Yu Yamanaka, Sho Matsugano, Yasunaga Yoshikawa, Koichi Orino
• Format: Article
• Language: English
• Published: MDPI AG 2016-05-01
• Series: Antibodies
• Subjects: immunoglobulin G; mammals; EDTA; fibrinogen; zinc ion
• Online Access: http://www.mdpi.com/2073-4468/5/2/13

Human immunoglobulin G (IgG) binding with zinc ions was examined using zinc ions immobilized on chelating Sepharose beads (Zn-beads). Human IgG bound to Zn-beads but not to Sepharose beads (control beads). Mouse, rat, bovine and equine IgGs also bound to Zn-beads, similar to human IgG. The human IgG F(c) fragment showed zinc ion–binding activity whereas the Fab fragment did not. Ethylenediaminetetraacetic acid (EDTA)-treated Zn-beads no longer bound human IgG; however, washing the beads, followed by the addition of zinc ions, restored the binding activity towards human IgG. Zn-beads saturated with human fibrinogen could bind human IgG, and Zn-beads saturated with human IgG could bind fibrinogen. These results suggest that animal IgGs, including human, specifically bind zinc ions, probably through a zinc-binding site in the F(c) fragment and not in the Fab fragment. In addition, IgG and fibrinogen interact with each other and/or bind zinc ions through different mechanisms.