NDLI: Improvement of the CuZn-superoxide dismutase enzyme activity and stability as a therapeutic agent by modification with polysialic acids

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Improvement of the CuZn-superoxide dismutase enzyme activity and stability as a therapeutic agent by modification with polysialic acids

Content Provider	Springer Nature Link
Author	Wu, Jian Rong Lin, Yi Zheng, Zhi Yong Lin, Chi Chung Zhan, Xiao Bei Shen, Ying Qiang
Copyright Year	2010
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.
Starting Page	1939
Ending Page	1945
Page Count	7
File Format	PDF
ISSN	01415492
Journal	Biotechnology Letters
Volume Number	32
Issue Number	12
e-ISSN	15736776
Language	English
Publisher	Springer Netherlands
Publisher Date	2010-09-05
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Coupling modification CuZn-SOD Enzyme stability Polysialic acids Biochemistry Applied Microbiology Biotechnology Microbiology
Content Type	Text
Resource Type	Article
Subject	Medicine Bioengineering Applied Microbiology and Biotechnology Biotechnology

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