Streptococcal antitumor protein: Expression in Escherichia coli cells and properties of the recombinant protein.
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- KANAOKA Masaharu
- Takarazuka Research Center, Sumitomo Chemical Co., Ltd.
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- NEGORO Takaharu
- Takarazuka Research Center, Sumitomo Chemical Co., Ltd. Present address: Sumitomo Pharmaceuticals Co., Ltd.
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- KAWANAKA Chigusa
- Takarazuka Research Center, Sumitomo Chemical Co., Ltd.
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- AGUI Hideo
- Takarazuka Research Center, Sumitomo Chemical Co., Ltd. Present address: Sumitomo Pharmaceuticals Co., Ltd.
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- NABESHIMA Shigeyasu
- Takarazuka Research Center, Sumitomo Chemical Co., Ltd.
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Streptococcal antitumor protein (SAGP) was produced by transformed E. coli 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 IC50 of the recombinant SAGP was 0.3 μ/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.
収録刊行物
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- Agricultural and Biological Chemistry
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Agricultural and Biological Chemistry 55 (3), 743-750, 1991
公益社団法人 日本農芸化学会
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詳細情報
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- CRID
- 1390282681441792000
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- NII論文ID
- 110006325427
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- NII書誌ID
- AA00515312
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- ISSN
- 18811280
- 00021369
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- PubMed
- 1368629
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- Crossref
- PubMed
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