Streptococcal Antitumor Protein: Expression in Escherichia coli Cells and Properties of the Recombinant Protein(Biological Chemistry)

概要

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Streptococcal antiturnor protein(SAGP) was produced by transformed E. coll JM103 carrying the SAGP gene downstream from the tac promoter. The purified recombinant SAGP had the same N-terminal amino acid sequence as that of the native SAGP isolated from Streptococcus pyogenes Su cells. Gel filtration analysis showed that the recombinant SAGP was a dimer, while the native SAGP was a tetramer. When the antitumor activity was tested against sarcoma 180 cells, the IC_<50> of the recombinant SAGP was 0.3 μg/ml, about a quarter as active as the native SAGP. These results suggest that the quaternary structure of SAGP is important for the antitumor activity.
社団法人日本農芸化学会の論文
1991-03-23