Pub No:
129
Title:
Ferrochelatase: Isolation and Purification via Affinity Chromatography
Authors:
Mailer, K., Poulson, R., David Dolphin, and Hamilton, A.D.
Journal:
Biochem. Biophys. Res. Commun.
Year:
1980
Pages:
96, 777-784
Abstract:
Ferrochelatase (EC 4.99.1.1) 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.

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