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. 2016 Sep 23;67(19):5799–5809. doi: 10.1093/jxb/erw345

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© The Author 2016. Published by Oxford University Press on behalf of the Society for Experimental Biology.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. 4. — Specific chitinase activity of native and alternatively spliced PR3b. (A) Conserved α-helixes (blue arrows), β-sheets (pink bars), and amino acids (red characters) of PR3b compared with the catalytic cores of GH18 family chitinases (Hurtado-Guerrero and van Aalten, 2007). The region affected by alternative splicing is underlined with a black line. (B) Purified proteins of GST-tagged PR3b and GST separated by SDS-PAGE gel. ‘GST-PR3b’ is the GST-tagged protein of native PR3b; ‘GST-PR3b Spliced’ is the GST-tagged protein of spliced PR3b. Marker is the protein standard ruler. The picture shown is a combination of representative lanes from gels with serial elutions of the purified proteins. (C) Enzyme-specific activity of GST-tagged native and alternatively spliced PR3b. One unit equals 1 μmol of released 4-MU. GST is used for the control reaction. Values are the average of three replicates. Error bar, mean ±SD. The asterisk indicates a significant difference between the paired data sets (P <0.05, Student’s t test).