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Antibodies 2016, 5(2), 13;

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

Laboratory of Veterinary Biochemistry, School of Veterinary Medicine, Kitasato University, Aomori 034-8628, Japan
Author to whom correspondence should be addressed.
Academic Editor: Roland Kontermann
Received: 4 March 2016 / Revised: 28 April 2016 / Accepted: 12 May 2016 / Published: 19 May 2016
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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. View Full-Text
Keywords: immunoglobulin G; mammals; EDTA; fibrinogen; zinc ion immunoglobulin G; mammals; EDTA; fibrinogen; zinc ion

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Yamanaka, Y.; Matsugano, S.; Yoshikawa, Y.; Orino, K. Binding Analysis of Human Immunoglobulin G as a Zinc-Binding Protein. Antibodies 2016, 5, 13.

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