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. 2019 Sep 17;11(8):1492–1501. doi: 10.1080/19420862.2019.1662690

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© 2019 The Author(s). Published with license by Taylor & Francis Group, LLC.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

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Figure 1. — Monomeric and multimeric Z_Ca variants with C-terminal cysteines analyzed as ligands in a column purification setup and by SPR (a) The average amount (±SD) of human polyclonal IgG eluted with EDTA at pH 5.5 from columns coupled with the mono- (red), di- (blue), tri- (yellow) and tetrameric (green) Z_Ca, based on triplicate experiments. The multimeric variants of Z_Ca capture significantly more protein as compared to the monomer (*P < .001). (b) Sensorgrams from triplicate injections of 500 nM IgG flown over surfaces with equimolar amounts of each Z_Ca variant immobilized show that larger multimers exhibit improved binding performance.