Ferrochelatase (protoheme ferro-lyase, EC 18.104.22.168) 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 molecular weight was 63,000 daltons; purified ferrochelatase ferro-lyase activity had a t1/2 (4° or −20°) of approximately 12 hours in the presence of beta-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.
ASJC Scopus subject areas
- Molecular Biology