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. Author manuscript; available in PMC: 2016 Jul 11.
Published in final edited form as: Arch Biochem Biophys. 2008 Mar 10;474(1):109–118. doi: 10.1016/j.abb.2008.02.043

Table 5.

Yield of heterodimer protein peak from the Ni-NTA column in the presence of various synthetic GST pi peptidesa

GST pi peptides Peak II (heterodimer)
Total Abs280 nm units Total GST activity unitsb (ΔOD340 nm/min)
1. None 1.18 1.36
2. Residues 41-85 No peak No peak
3. Residues 115-124 No peak No peak
4. Residues 131-163 0.49 0.62
5. Residues164-197 0.66 0.74
6. Residues 32-40 1.10 1.21
7. Residues 86-97 0.94 1.09
a

GST pi and 1-Cys Prx proteins (40 μM of each) together with 100 μM of synthetic GST pi peptide were treated with 20% 1,6-hexanediol followed by dialysis against buffer containing 2.5 mM GSH and loaded onto a Ni-NTA column, as described in Materials and methods.

b

GST activity was measured using CDNB as the electrophilic substrate, as described in Materials and methods, and expressed as ΔOD340 nm/min.