폐렴구균 열충격 단백질 GroEL의 특성 = Charaterization of GroEL Homolog from Streptococcus pneumoniae

다국어 초록 (Multilingual Abstract)

Induction and purification of the GroEL homolog from Streptococcus pneumolliae were characterized. The stress conditions were determined by temperature, ethanol, NaCI, $H_2O_2$ methyl methanesulfonate, and ethyl methanesulfonate. And stress induced proteins were analyzed using [$^{35}S$]-methionine labeling method. Heat shock induced the synthesis of a set of about 3 heat shock proteins (hsps) (65, 73, and 84-kDa). Of those 3 hsps, a 65 kDa protein, hsp65, was purified by DEAE-Sephacel and ATP-agarose column chromatography, and used for antibody preparation. Immunoblot analysis employing antisera raised against pneumococcus hsp65 demonstrated cross-reactivity with a 60 kDa protein in Eschericha coli. Also cross reaction of the purified p65 with anti-Escherichia coli GroEL monoclonal antibody demonstrated that pneumococcal hsp65 is the GroEL homolog.