Additional file 2: Figure S2.
Cathepsin S and B substrates are cleaved by both enzymes. Cathepsin B and S activity was measured in crude PBMC lysate resuspended in pH 4.0 using fluoregenic subtrates. When using inhibitors, lysate was preincubated with Cathepsin S, D, K, B and an omnicathepsin inhibitor following which activity of the enzyme was measured. The average maximum slope of the curve derived from three replicates quantified in relative fluorescent units (RFU)/min is plotted.
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Vaithilingam et al. BMC Cell Biology 2013 14:35 doi:10.1186/1471-2121-14-35