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. 2016 Feb 20;63(1):13–18. doi: 10.5458/jag.jag.JAG-2015_012

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2016 by The Japanese Society of Applied Glycoscience

This is an open-access paper distributed under the terms of the Creative Commons Attribution Non-Commercial (by-nc) License (CC-BY-NC4.0: https://creativecommons.org/licenses/by-nc/4.0/).

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Fig. 1. — Purification of xyloglucanases from V. dahliae.

(A) Elution profile of Butyl Toyopearl column chromatography. Thick bars a and b corresponded to the activities of XEG12A and XEG74B, respectively. Every 10 mL of the effluents were collected per a tube. (B) SDS-PAGE of purified XEG12A and XEG74B (right lane of each gel). Total 20 μg of the purified enzymes were applied. M; molecular markers. (C) Deglycosylation of XEG12A and XEG74B. The symbols minus and plus are without and with glycopeptidase F treatment, respectively. Gels were stained with Coomassie Blue.