Abstract
The expression in eukaryotic cells of heat shock proteins (Hsps) is induced by various stresses such as burn, infection, inflammation, and exposure to carcinogens or heavy metals. Hsp70 genes (hsp70) were isolated from human cDNA and were inserted into E. coli. Hsp70 proteins were separated from the inclusion bodies in E. coli expressing Hsp70 and were purified by sonication, detergents (Triton-X and urea) and sequential chromatography on Sephacryl S-200 and Resource Q column. Anti-Hsp70 antibodies in sera of burn patients (burn group) were measured by Western blot and enzyme-linked immunosorbent assey (ELISA) with purified Hsp70 protein as the antigen. Control sera were taken from multiple trauma or hemorrhagic shock patients (stress group) and from normal adults (control group). The results showed that the anti-Hsp70 antibody titers of the IgG class were significantly elevated in both the burn patients (0.71±0.46) and the stress group (0.70±0.42) in comparison with the control group (0.42±0.43). Furthermore, the anti-Hsp70 antibody titers of IgG class in the sera of burn patients tend to negatively correlate with the degree of burn surface area.
