Ferrochelatase: Isolation and purification via affinity chromatography

K. Mailer, R. Poulson, D. Dolphin, A. D. Hamilton

Research output: Contribution to journalArticle

Abstract

Ferrochelatase (protoheme ferro-lyase, 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 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.

Original languageEnglish (US)
Pages (from-to)777-784
Number of pages8
JournalTopics in Catalysis
Volume96
Issue number2
DOIs
StatePublished - 1980

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Biophysics
  • Molecular Biology

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