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. Author manuscript; available in PMC: 2011 Jul 1.
Published in final edited form as: J Insect Physiol. 2010 Feb 2;56(7):736–744. doi: 10.1016/j.jinsphys.2010.01.003

Fig. 3.

Fig. 3

Protein alignment of serine proteases. Protein alignment of all serine proteases used in this analysis from positions ~170–220. Numbering is based on bovine α-chymotrypsinogen. Residues of importance are represented as follows; (*) Ser195 catalytic triad residue, (◆) accessory catalytic residues, (▲) the third and final disulfide bridge and (Δ) Asp194 where position 1 (Ile/Val) becomes buried following activation of the mature peptide.