Abstract
Abstract A fast protein liquid chromatographic method for purification of selenium-containing allophycocyanin (Se-APC) from selenium-enriched Spirulina platensis was demonstrated in this study. The purification procedures included ammonium sulphate precipitation and hydroxylapatite chromatography. Highly pure Se-APC with Se concentration of 415.7 μg g−1 protein was finally obtained. In haemolysis assay, increase in MDA content and ROS generation were found in erythrocytes exposed to t-BOOH. Se-APC exhibited higher antioxidant activity and better protective effect than APC on erythrocytes against t-BOOH-induced oxidative damage. Morphological change of erythrocytes as detected by atomic force microscopy was effectively reversed by Se-APC. In the hepatoprotective model, cytotoxicity induced by t-BOOH in HepG2 cells was significantly attenuated by Se-APC. The studies on the mechanism revealed that Se-APC could block the t-BOOH-induced apoptosis and G2/M cell cycle arrest. The findings suggest that Se-APC is a promising seleno-protein with potential applications in treatment of diseases related with oxidative stress.
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