Figure 5. Hydrolysis of bovine serum albumin and hemoglobin by SmCL3.

Recombinant SmCL3 (∼100 nM) was incubated with serum albumin (A) or bovine hemoglobin (B) overnight at 37°C in 50 mM citrate, 100 mM sodium phosphate (pH 3.0–7.0) or 100 mM glycine (pH 8.0–10.0.) buffers containing 2 mM DTT. Some cleavage can be observed across the whole pH spectrum. Cleavage was optimal for both protein substrates between pH 4.0–7.0. (C) Samples incubated at pH 5.0, but without the presence of protease.