Ferrochelatase: Isolation and Purification via Affinity Chromatography
Mailer, K., Poulson, R., David Dolphin, and Hamilton, A.D.
Biochem. Biophys. Res. Commun.
Ferrochelatase (EC 184.108.40.206) from rat liver has been purified by affinity chromatography. Synthesis of the affinity column ligand and a preliminary investigation of enzyme properties are reported. The SDS-gel electrophoresis mol. wt. was 63,000 daltons; purified ferrochelatase ferro-lyase activity had a t1/2 (4 oC or -20 oC) of approximately 12 h in the presence of β-mercaptoethanol. Addition of CuCl2 to the purified enzyme resulted in a decrease in activity contrary to the previously reported increase in activity with crude enzyme.