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. 2010 Dec 14;1(5):e00285-10. doi: 10.1128/mBio.00285-10

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Copyright © Moraïs et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-Share Alike 3.0 Unported License, which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original author and source are credited.

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FIG 2 — Electrophoretic mobility of components and assembled complexes on nondenaturing and denaturing gels. For the two xylanase gels, equimolar concentrations of the chimeric enzymes (11A-xbm-a and 10B-t) and their matching divalent scaffoldin (Scaf·AT) were combined. For the two cellulase gels, equimolar concentrations of the chimeric enzymes (f-5A and b-48A) and their matching divalent scaffoldin (Scaf·BF) were combined. For the two mixed-enzyme complex gels, equimolar concentrations of the chimeric enzymes (f-5A, b-48A, 11A-xbm-a, and 10B-t) and their matching tetravalent scaffoldin (Scaf·BTAF) were combined. The single fusion proteins and the mixtures were subjected to nondenaturing PAGE (A) and denaturing SDS-PAGE (B). Analysis of the matching components by nondenaturing PAGE indicates their near-complete interaction as a single major band formed. The schematic representations below the gels are explained in the symbol key in Fig. 1 and in the legend to Fig. 1.