Figure 5: Binding of Cry2Aa to recombinant peptides.
From: Proteomic analysis of Cry2Aa-binding proteins and their receptor function in Spodoptera exigua
(a) Positions of purified, recombinant peptides after staining with Coomassie Blue on SDS–PAGE gel. Peptides had been bacterially expressed and purified in a nickel-nitrilotriacetic acid (Ni-NTA) affinity column. Lanes 1 to 8 are: the Se-V-ATPase subunit A, Se-V-ATPase subunit B, Se-actin, Se-4-HB-CoAT, Se-Rack, and three truncated recombinant Se-polycalin peptides (6 = peptide1, 7 = peptide2, 8 = peptide3). (b) Degree of binding, as indicated by optical density (OD), of Cry2Aa to different Se-peptide fragments. Se-V-ATPase subunit A (■), Se-V-ATPase subunit B (♦), Se-actin (▲), Se-4-HB-CoAT (★), Se-Rack (○), Se-polycalin peptide1 (◇), Se-polycalin peptide2 (▼) and Se-polycalin peptide3 (●).
