Skip to main content
. Author manuscript; available in PMC: 2010 Jan 11.
Published in final edited form as: Biopolymers. 2008 Nov;89(11):960–968. doi: 10.1002/bip.21043

Figure 2.

Figure 2

Chromatogram of the separation of N-TIMP-1 by high-resolution cation exchange chromatography. N-TIMP-1 (10 mg) purified by cation exchange chromatography with CM-52 was loaded onto a new Mono S HR 5/5 cation exchange column pre-equilibrated with buffer A (20 mM Bis Tris-HCl, pH 5.5). The column was then washed with 10 mL buffer A, and bound protein was eluted with a linear gradient of 0–100% buffer B (20 mM Bis Tris-HCl, pH 5.5, 0.5 M NaCl) over 60 minutes at a flow rate of 1mL/min. The two components are labeled peaks 1 and 2, respectively.