Figure 4
From: Characterization of vaccinia virus A12L protein proteolysis and its participation in virus assembly
![Figure 4](http://media.springernature.com/full/springer-static/image/art%3A10.1186%2F1743-422X-4-78/MediaObjects/12985_2007_Article_291_Fig4_HTML.jpg)
The predicted molecular weights and pI's of potential A12L cleavage products. The schematic cleavage products at each AG/X site were drawn with the molecular weights of 6, 6.5, 3.6, and 4.4 kDa. Utilizing single and double AG/X sites, proteolytic processing of A12L were predicted as follows: cleavage at the middle AG/K site would only produce a 12 kDa and a 8 kDa peptide, while cleavages at the C-terminus AG/K site and the N-terminus AG/A site only would introduce a 16 kDa and a 15 kDa product (bottom), respectively. The utilization of both AG/A and N-terminal AG/K site would generate a 10 kDa peptide.