Figure - PMC

Skip to main content

View full-text article in PMC

. Author manuscript; available in PMC: 2012 Dec 4.

Published in final edited form as: Int J Biochem Cell Biol. 2009 Feb 20;41(7):1601–1612. doi: 10.1016/j.biocel.2009.02.003

Fig. 4 — A: FhcatB1 was incubated in AMT buffers at various pH values, following which the residual activity at pH 4.5 was determined against Z Phe Arg AMC (t_½ is represented by the closed squares). The activity of FhcatB1 was measured against FITC-casein at different pH values (activity values represented by open diamonds). B: Activity of human cathepsin B enzymes and FhcatB1 against exopeptidase substrates. The initial velocities for human wild-type (open bars), His110Ala cathepsin B (grey bars) and FhcatB1 (dark bars) are plotted as AFU/min/nM enzyme. To aid visualization, a break has been introduced between 15 and 40 AFU/min/nM enzyme.

Fig. 4 — A: FhcatB1 was incubated in AMT buffers at various pH values, following which the residual activity at pH 4.5 was determined against Z Phe Arg AMC (t_½ is represented by the closed squares). The activity of FhcatB1 was measured against FITC-casein at different pH values (activity values represented by open diamonds). B: Activity of human cathepsin B enzymes and FhcatB1 against exopeptidase substrates. The initial velocities for human wild-type (open bars), His110Ala cathepsin B (grey bars) and FhcatB1 (dark bars) are plotted as AFU/min/nM enzyme. To aid visualization, a break has been introduced between 15 and 40 AFU/min/nM enzyme.