Figure 3
From: Using phage display technology to obtain Crybodies active against non-target insects
Solubilization and trypsin treatment of protoxin variants. Coomassie blue stained 12% acrylamide gel showing solubilized protein treated (+) and untreated (−) with trypsin. Cry1Aa13 wild type was used as positive control for solubilisation (lane wt −) and trypsin activation (lane wt +). Lanes A8, A10, A11 and A12 show the solubilized Cry1Aa13-A8, Cry1Aa13-A10, Cry1Aa13-A11 and Cry1Aa13-A12 respectively. Trypsin-treated toxins exhibited a protein of 65 kDa corresponding to the core of the toxin or activated toxin. Cry1Aa13-A11 showed the same band but less intense than the rest of the mutants. Arrows A and B indicate the molecular weight of the approximately 37 kDa and 28 kDa fragments observed during trypsin digestion.
