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《Journal of Yunnan Agricultural University(Natural Science)》 2013-06
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Expression,Purification and Characterization of Recombinant Human Heme Oxygenase 2 in Escherichia coli

ZHOU Chuanwen;LI Yipeng;DING Yu;School of Life Sciences,Fudan University;  
Heme oxygenase is an enzyme that catalyzes the degradation of heme,and then produces biliverdin,iron ion,and carbon monoxide. Although heme oxygenase-2( HMOX2) had similar oxygenase activity as HMOX1,their cellular distribution and reaction kinetics are different. Compared to HMOX1,there are few research focused on HMOX2. In this article,we first cloned human HMOX2 to the pT7 high expression level vector from human cDNA,then we overexpressed HMOX2 by the auto-induction system. The expressed recombinant His 10-HMOX2 was purified by Ni-NTA affinity chromatography and Mono Q anion exchange chromatography. The typical yield of recombinant HMOX2 was 92. 6 mg from 1 liter culture medium with purity about 92 %. The recombinant HMOX2 was assayed for oxygenase activity, showing oxygenase activity of 69. 51 u / mg. The oxygenase activity assay also showed that the purified HMOX2 tolerated broad ranges of pH( pH 6 ~ 9) and temperature( 20 ~ 95 ℃). The optimum temperature and pH is 40 ℃ and pH 8. Our research may facilitate further research of HMOX2 ' s biochemical activity and its role in the related diseases.
【Fund】: 国家自然科学基金项目(30500113)
【CateGory Index】: Q55
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