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. 2011 Oct 11;63(2):913–924. doi: 10.1093/jxb/err320

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© 2011 The Author(s).

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

This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

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Fig. 5. — Profile of activity of proteins isolated from ABA-treated (10 h) and untreated roots after fractionation through a Sephacryl S-200 column and western blot analysis evaluating the presence of SnRK1 and SnRK2 in fractions from the column. Activity was evaluated using AMARA, AREBP1, and AREBP2 as substrates in the absence or presence of 1 mM CaCl₂. SnRK1 antiserum was raised against a peptide from the catalytic domain of SnRK1 (Fragoso et al., 2009) while SnRK2 antiserum was raised to a peptide from a highly conserved region in SnRK2. (A) Activity profile of proteins from ABA-untreated roots, no calcium added. (B) As for (A) with calcium added. (C) Western blot analysis evaluating the presence of SnRK1 and SnRK2 in ABA-untreated roots. (D) Activity profile of proteins from ABA-treated roots, no calcium added. (E) As (D) with calcium added. (F) Western blot analysis evaluating the presence of SnRK1 and SnRK2 in ABA-treated roots. The 42 kDa SnRK2 is indicated with an arrow. Fraction numbers are indicated and the positions of 39 and 64 kDa molecular-mass markers are shown in (C) and (F).