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. 2018 Apr 13;13(4):e0195077. doi: 10.1371/journal.pone.0195077

Fig 1. Analysis of the human cathepsin G preparation used in the determination of the extended cleavage specificity.

Fig 1

The enzyme had previously been purified from blood neutrophils and the purity of the preparation was determined by separation on SDS-PAGE and visualized with Coomassie Brilliant Blue staining. In panel A commercial preparations of two additional neutrophil proteases N-elastase (NE) and proteinase 3 (P3) were also included in the figure for comparison. Proteinase 3 and hCG were intact after short term storage at +4°C. However, N-elastase showed several degradation products indicating self-cleaving activity. In panel B three additional enzymes, the human mast cell chymase (HC), human thrombin (Th) and human granzyme B (GB) were included as they were used as reference proteases in the chromogenic and recombinant substrate assays.