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Updated: Jun 3, 2026
Radiochemical Assessment of Glycogen Synthase Enzyme Activity in Animal Tissue
Published on: October 24, 2025
[Comparison of two techniques for expression and purification of glycogen synthase kinase 3β]
Shao-fei XU1, Jie XU, Ming-tao LI
1Proteomics Center, Zhongshan School of Medicine, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou 510080, China. sfeixu@126.com
Objective:
To establish a method for the expression of glycogen synthase kinase 3β with high purity and biological activity.
Methods:
E.coli expression system and baculovirus-insect cell expression system were used to produce the kinase, followed by purification using His-tag and GST-tag and determination of its purity and activity by SDS-PAGE and kinase reaction, respectively.
Results:
Glycogen synthase kinase 3β produced from E.coli represented 54% of the total bacterial protein, as compared with 96% of the total protein from the insect cell system .Glycogen synthase kinase 3β produced from insect cell exhibited an one-fold higher biological activity than the protein obtained from E.coli.
Conclusions:
Compared with the protein from E.coli system, glycogen synthase kinase 3β from the insect cell expression system is endowed with a higher purity and bioactivity.
