Nickel and copper complexes of a chelating methacrylate sorbent in the purification of chitinases and specific immunoglobulin G1 by immobilized metal ion affinity chromatography.

The isolation of the isoforms of endo- and exochitinases of Clostridium aminovalericum T1 and of the horseradish peroxidase (HRP)-specific immunoglobulin G1 from natural sources by immobilized metal ion affinity chromatography was studied. The effect of Cu2+ and Ni2+ complexes of iminodiacetic acid incorporated in porous glycidyl methacrylate-co-ethylene dimethacrylate and in agarose (Sepharose Fast Flow) beads on separation of the target polypeptides was analyzed. It was found that the Cu2+ complexes bound both the HRP-specific IgG1 and some isoforms of chitinases more strongly than the Ni2+ complexes.