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. 2015 Nov 4;15:257. doi: 10.1186/s12866-015-0582-6

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© Manohar and Acharya. 2015

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 3 — Purification and biochemical analysis of PCNAs. The wild type and mutant PCNAs were purified and ~1 μg of each protein was analyzed. a . Purified proteins were resolved in SDS-12 % polyacrylamide gel. Lanes 1, Molecular weight standards; 2, ScPCNA; 3, CaPCNA; and 4, CaPCNA G178S. c. Purified proteins were resolved in 12 % non-denaturing polyacrylamide gel. Lanes 1, CaPCNA; 2, CaPCNA G178S; and 3. ScPCNA. c. Size exclusion chromatograms of wild type (blue) and G178S mutant (red) CaPCNAs with the peak fractionation at ~1.6 ml and ~2.3 ml elution volume, respectively, were shown. d. Glutaraldehyde crosslinked 20 μg of CaPCNA (lane 2) or CaPCNA G178S (lane 3) or ScPCNA G178S (lane 4) proteins were resolved in SDS-12 % polyacrylamide gel. Monomer (~29 kDa) and oligomeric PCNAs (~60-180 kDa) are marked. Lane 1, Molecular weight standards.