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Antibodies 2016, 5(2), 13; doi:10.3390/antib5020013

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
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Academic Editor: Roland Kontermann
Received: 4 March 2016 / Revised: 28 April 2016 / Accepted: 12 May 2016 / Published: 19 May 2016
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Abstract

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
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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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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