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- W2361788939 abstract "AIM: To investigate the activity of MIP4 mutant (Met MIP4) in blocking eosinophils chemotaxis in vitro by expressing Met MIP4 in E. coli and purifying it. METHODS: The gene of Met MIP4 was inserted into the expression vector pRSET A and pRSET Met MIP4 fusion protein was expressed by IPTG induction. After E. coli . was lysed by ultrasonic wave, the solubility of the fusion protein was determined by SDS PAGE gel electrophoresis. Protein in supernatant was purified by Ni 2+ NTA agarose beads. The activity of pRSET Met MIP4 protein in inhibiting eosinophils chemotaxis was determined with 24 well chemotaxis plate filter. RESULTS: The pRSET Met MIP4 fusion protein was expressed in E. coli . The solubility of the fusion protein reached 80% and the purity of the fusion protein was 87% by Ni 2+ NTA agarose beads. Eosinophil was purified from asthmatic blood and Eosinophil purity was 90%. Investigation of biological function of the fusion protein showed that the fusion protein inhibited the eosinophils chemotaxis. CONCLUSION: The pRSET Met MIP4 protein has been correctly expressed in E. coli and the fusion protein is soluble. Study of the biological function of the fusion protein indicates that the fusion protein can inhibit eosinophils chemotaxis in vitro ." @default.
- W2361788939 created "2016-06-24" @default.
- W2361788939 creator A5068574525 @default.
- W2361788939 date "2003-01-01" @default.
- W2361788939 modified "2023-09-23" @default.
- W2361788939 title "Inhibition of eosinophil chemotaxin by mutant of macrophage inflammatory protein 4" @default.
- W2361788939 hasPublicationYear "2003" @default.
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