Figure 1

Chromatography of SCP on Sephadex G-100 and FPLC SP-Sepharose. (A) Chromatography of SCP on Sephadex G-100. The column (3.2 × 100 cm) was equilibrated with buffer A (10 mM acetate pH 6, 10 mM NaCl and 4 mM CaCl₂). The elution of protease was performed with the same buffer at a rate of 30 mL/h and 5.6 mL by fraction. (B) Chromatography of SCP on FPLC SP-Sepharose. The column was equilibrated with buffer A (10 mM Tris-HCl pH 8, 10 mM NaCl and 4 mM CaCl₂); a linear gradient was applied from 10 to 120 mM NaCl in buffer B; the elution of protease was performed with the same buffer at a rate of 2 mL/min and 3 mL by fraction. C: Chromatography of SCP on Sephadex G-50. The column (3 × 90 cm) was equilibrated with buffer A. The elution of protease was performed with the same buffer at a rate of 30 mL/h and 4.8 mL by fraction. SCP activity was measured as described in materials and methods section using casein as substrate. SCP activity was measured as described in materials and methods section using casein as substrate.