Background and the purpose of the study: Heat Shock Protein 90 (Hsp90) is typically the most
abundant chaperone in the eukaryotic cell cytoplasm, and its expression is essential for loading
immunogenic peptides onto major histocompatibility complex molecules for presentation to Tcells.
Therefore, it may act as a good candidate as an adjuvant molecule in vaccine technology.
Methods: Initially the human Hsp90β gene was cloned into the heat inducible expression vector
pGP1-2 and then the recombinant protein was isolated by ion exchange chromatography. After
intradermal injection of confirmed purified band of protein to rabbits and isolation of the serum
IgG antibody, for its affinity purification, the rabbit’s purified Hsp90 specific IgG was coupled
to the cyanogen bromide-activated Sepharose 4B.
Results: The recovery of the purified protein of interest by affinity chromatography was 50% .
Conclusion: This research enabled purification of human heat shock protein by a laboratory
prepared column chromatography.
کلید واژگان :
CNBr activated Sepharose 4B; Head shock protein 90(Hsp90); Rabbit IgG; pGP1-2
