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

作者：Pleonsil Pornthip; Soogarun Suphan; Suwanwong Yaneenart^*

来源：International Journal of Biological Macromolecules, 2013, 60: 393-398.

DOI：10.1016/j.ijbiomac.2013.06.016

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

This study was conducted to investigate the anti-oxidant activity of the recombinant apo-c-phycocyanin (c-PC) beta-subunit compared to native c-PC purified from Spirulina sp. The gene encoding the beta-subunit of c-PC was successfully cloned and expressed in Escherichia coli. The anti-oxidant capacities of recombinant apo-c-PC(beta) 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 antioxidant capacities are native c-PC %26gt;%26gt; Trolox %26gt; recombinant apo-c-PC(beta). 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.

• 出版日期2013-9