Ferrochelatase: Isolation and purification via affinity chromatography

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

doi:10.1016/0006-291X(80)91422-9

Ferrochelatase: Isolation and purification via affinity chromatography

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

Chemistry

Research output: Contribution to journal › Article › peer-review

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 t_1/2 (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 language	English (US)
Pages (from-to)	777-784
Number of pages	8
Journal	Topics in Catalysis
Volume	96
Issue number	2
DOIs	https://doi.org/10.1016/0006-291X(80)91422-9
State	Published - 1980

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Biophysics
Molecular Biology

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10.1016/0006-291X(80)91422-9

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title = "Ferrochelatase: Isolation and purification via affinity chromatography",

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.",

author = "K. Mailer and R. Poulson and D. Dolphin and Hamilton, {A. D.}",

year = "1980",

doi = "10.1016/0006-291X(80)91422-9",

language = "English (US)",

volume = "96",

pages = "777--784",

journal = "Topics in Catalysis",

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T1 - Ferrochelatase

T2 - Isolation and purification via affinity chromatography

AU - Mailer, K.

AU - Poulson, R.

AU - Dolphin, D.

AU - Hamilton, A. D.

PY - 1980

Y1 - 1980

N2 - 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.

AB - 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.

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JO - Topics in Catalysis

JF - Topics in Catalysis

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ER -

Ferrochelatase: Isolation and purification via affinity chromatography

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