Expression and activity of vMIP-Ⅱ in single strand of blocking to chemokine receptors / 中国免疫学杂志
Chinese Journal of Immunology
;
(12)2000.
Article
in Chinese
| WPRIM
| ID: wpr-537184
ABSTRACT
Objective:
To establish an efficient method for expression and purification of vMIP-Ⅱ which encoded by a viral gene and ho-mogued human chemokine in active single strand in E.coli cells.Methods:
Cloning with bi-enzyme restriction and lysising bacteria with cold osmoic shock were used for expression,MBP affinity chromatography of fusion protein and self-selective of recombinative peptide for final purification. The expressing and purifying products were detected with SDS-PAGE and Western blotting and identified with inhibitory adhesion experiment for its activity.Results:
Fusion protein MBP-vMIP was effeciendy expressed in E. coli at secretive type, and self-cleaved to sparate the vMIP-Ⅱ. The final product single strand vMIP-Ⅱ was active for blocking chemokine receptor CCR5.Conclusion:
This is an effective method for obtaining viral chemokine vMIP-Ⅱ of recombinant single strand.The recombinant vMIP-Ⅱ may be useful for the study of diseases involving in chemokiine receptors such as HIV infection,rejection of transplantation and chronic inflammation,etc.
Full text:
Available
Index:
WPRIM (Western Pacific)
Language:
Chinese
Journal:
Chinese Journal of Immunology
Year:
2000
Type:
Article
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