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Int J Biol Macromol. 2013 Sep;60:393-8. doi: 10.1016/j.ijbiomac.2013.06.016. Epub 2013 Jun 24.

Anti-oxidant activity of holo- and apo-c-phycocyanin and their protective effects on human erythrocytes.

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Graduate Program of Clinical Haematology Sciences, Department of Clinical Microscopy, Faculty of Allied Health Sciences, Chulalongkorn University, Bangkok 10330, Thailand.


This study was conducted to investigate the anti-oxidant activity of the recombinant apo-c-phycocyanin (c-PC) β-subunit compared to native c-PC purified from Spirulina sp. The gene encoding the β-subunit of c-PC was successfully cloned and expressed in Escherichia coli. The anti-oxidant capacities of recombinant apo-c-PC(β) and native c-PC were evaluated by measuring their Trolox equivalent antioxidant capacities and examining their protective effects on erythrocytes from normal and homozygous haemoglobin E individuals against peroxyl radicals and hydrogen peroxide. The results demonstrated that the anti-oxidant capacities are native c-PC≫Trolox>recombinant apo-c-PC(β). Both anti-oxidant proteins can potentially protect erythrocytes from oxidative damage. Expression of c-PC in bacteria reduces the cost and time for protein production, and the recombinant protein could be further developed to obtain a more efficient protein for therapeutic purposes.


Anti-oxidant; Erythrocyte; Haemoglobin E; Phycocyanin; Recombinant protein

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