Anti-oxidant activity of holo- and apo-c-phycocyanin and their protective effects on human erythrocytes
Anti-oxidant activity of holo- and apo-c-phycocyanin and their protective effects on human erythrocytes
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DOI：
10.1016/j.ijbiomac.2013.06.016
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发表时间：
2013-09-01
影响因子：
8.2
通讯作者：
Suwanwong, Yaneenart
中科院分区：
文献类型：
--
作者：
Pleonsil, Pornthip;Soogarun, Suphan;Suwanwong, Yaneenart
本研究比较了从螺旋藻中纯化的重组apo-c-藻蓝蛋白(c-PC)β亚基和天然c-PC的抗氧化活性。成功克隆了c-PCβ亚基编码基因，并在大肠杆菌中进行了表达。通过测定重组apo-c-PC(β)和天然c-PC的Trolox当量抗氧化能力，以及检测它们对正常和纯合子Hb E个体红细胞对过氧化自由基和过氧化氢的保护作用来评价重组apo-c-PC(β)和天然c-PC的抗氧化能力。结果表明，重组apo-c-PC(β)具有天然c-PC>；这两种抗氧化蛋白质都可以潜在地保护红细胞免受氧化损伤。C-PC在细菌中的表达降低了蛋白生产的成本和时间，重组蛋白可以进一步开发以获得更有效的治疗用蛋白。(C)2013爱思唯尔B.V.保留所有权利。
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 >> Trolox > 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. (C) 2013 Elsevier B.V. All rights reserved.