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. 2016 Sep 7;5(3):36. doi: 10.3390/plants5030036

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© 2016 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC-BY) license (http://creativecommons.org/licenses/by/4.0/).

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Purification of napin from B. napus meal protein extract at pH 3. (A) Polypeptide profiles of meal and pH 3 extract after membrane filtration (MF); (B) Chromatograms of membrane-separated proteins further cleaned using HiTrap Phenyl Sepharose™ 6 Fast Flow Hydrophobic Interaction column (HIC); (C) Polypeptide profiles of napin after HIC; and (D) Native-PAGE separation of napin in (C). For SDS-PAGE, polypeptide profiles were under non-reducing (−ME) and reducing (+ME) conditions. Precast homogeneous gels of 20% and low range molecular weight markers (MWM) were used.