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Licensed Unlicensed Requires Authentication Published by De Gruyter June 3, 2015

A simple and highly sensitive method of measuring heme oxygenase activity

  • Pham Hieu Liem , Anfeng Mu , Shun-ichi Kikuta , Kazushi Ohta , Sakihito Kitajima and Shigeru Taketani EMAIL logo
From the journal Biological Chemistry


Heme oxygenase (HO) is a rate-limiting step of heme degradation, which catalyzes the conversion of heme into biliverdin, iron, and CO. HO has been characterized in microorganisms, insects, plants, and mammals. Previously used assays of HO activity were complicated and had low sensitivity. We found that the use of an eel bilirubin-bound fluorescent protein, UnaG, can achieve a highly sensitive and simple assay of HO activity. Using several enzyme sources including human culture cells, homogenates of plant tissues, and recombinant yeast HO, data were successfully obtained. The present method can facilitate the examination of HO in various organisms.

Corresponding author: Shigeru Taketani, Kyoto Institute of Technology, Department of Biotechnology, Kyoto 606-8585, Japan; and Department of Microbiology, Kansai Medical University, Hirakata, Osaka 573-1010, Japan, e-mail:


The authors thank Dr. Atsushi Miyawaki for a kind gift of pcDNA3-UnaG. This study was supported in part by grants from the Ministry of Health, Labor and Welfare of Japan.


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Received: 2015-5-6
Accepted: 2015-5-30
Published Online: 2015-6-3
Published in Print: 2015-11-1

©2015 by De Gruyter

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