Improvement of the CuZn-superoxide dismutase enzyme activity and stability as a therapeutic agent by modification with polysialic acids |
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Authors: | Jian Rong Wu Yi Lin Zhi Yong Zheng Chi Chung Lin Xiao Bei Zhan and Ying Qiang Shen |
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Institution: | (1) School of Biotechnology, Jiangnan University, Wuxi, 214122, People’s Republic of China;(2) Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, Wuxi, 214122, People’s Republic of China;(3) School of Materials Science and Engineering, Nanyang Technological University, 50 Nanyang Avenue, Singapore, 639798, Singapore |
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Abstract: | The optimal process for the polysialylation reaction was as follows: polysialicacid (PSA) was activated by periodate oxidation,
then coupled to CuZn superoxide dismutase (SOD) with a PSA:SOD molar ratio of 40:1 for 24 h. The resulting polysialylated
protein contained 3.9 ± 0.3 mol PSA per mol SOD. SDS-PAGE and atomic force microscopy revealed that the molecular weight of
polysialylated SOD was about 90–100 kDa. The average size was 10–15 nm, about four-fold of the native enzyme. Compared to
the native enzyme, the activity and stability of the polysialylated SOD, as well as resistance to heat, acid, alkali and proteases
present in human digestive system such as pepsin and trypsin, were improved significantly as therapeutic agent. |
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