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Design, construction and characterization of prourokinase mutant engineered by introduction of special Lys-Gly-Asp-Trp-motif

Author(s): Jian Jing

Journal: Advances in Biological Chemistry
ISSN 2162-2183

Volume: 03;
Issue: 02;
Start page: 164;
Date: 2013;
Original page

Keywords: Prourokinase | Lys-Gly-Asp-Trp-motif | Baculovirus-Insect Cell Expression System | Fibrinolytic Activity | Anti-Thrombosis Activity

A recombinant prourokinase chimera was constructed by introduction of Lys-Gly-Asp-Trp-motif between Gly118 and Ile119 among the kringle domain. The structure of designed protein was predicted and simulated. The recombinant prourokinase chimera was produced in insect cell sf9 with baculovirus-expression vector and existed as active form. Chimera protein was purified by affinity chromatography coupled with antibody. The special activity of the chimera was 90,000 IU/mg detected by fibrin plate determination. It was also shown that chimera inhibited ADP-induced platelet aggregation in a concentration depenent manner. These results showed the prourokinase chimera exhibited not only high fibrinolytic activity but also had anti-thrombosis function.
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