Analysis of the cleavage of a panel of consensus substrates for four human neutrophil proteases.

<p>The cleavage of a number of consensus cleavage sites for four different human neutrophil proteases (N-elastase, hCG, hPR3 and NSP4) were studied with the 2x-Trx system. The ‘A’ consensus sites come from phage display analyses performed in our lab and the substrates B and C comes from a proteomics study by O’Donoghue et al [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0195077#pone.0195077.ref036" target="_blank">36</a>]. The substrates originating from the two different methods for N-elastase and proteinase 3 both show very good cleavage, whereas for hCG the consensus sites obtained by the proteomics method shows only minor cleavage, indicating a relatively poor site. No phage display has yet been performed on hNSP4, therefore only a proteomics site was studied where minor cleavage after using a relatively high concentration of the enzyme was seen.