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. 2019 Aug 5;9:11324. doi: 10.1038/s41598-019-47815-z

Figure 2.

Figure 2

Effect of rFXIII-A calcium binding site mutants on its specific activity and substrate specificity. Panels a, b and c represent comparative bar graphs for Specific activity of intracellular lysates (wild type and variant) based on Photometric assay, interpolated FXIII-A activity based on Pentylamine incorporation assay and α-2 antiplasmin incorporation assay, respectively. In the event a variant is significantly different than the wild type, it is marked with a star (*) sign on top of the corresponding bar. Statistical significance is set at p < 0.05. Experiments were performed in duplicates, thrice (N = 6). Panel d shows the putative fibrinogen, α-2 antiplasmin and BAPA binding site residues on zymogenic FXIII-A monomeric and activated monomeric FXIII-A* structures along with two intermediate transition state structures. The structure backbone is depicted in grey colored ribbon format. The putative binding site region backbones are colored cyan for fibrinogen, yellow for BAPA and magenta for α-2 antiplasmin. The three calcium binding sites are also depicted on all four structures as stick models colored red (Cab1), blue (Cab2) and green (Cab3) respectively.