A New Potent Kinin-inactivating Enzyme from the Mushroom Psalliota hortensis
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概要
- 論文の詳細を見る
A new potent kinin-inactivating enzyme was purified from a kind of Japanese mushroom, Psalliota hortensis (Tsukuritake, in Japanese), by means of water extraction, ammonium sulfate fractionation, DEAE-Sephadex A-50 chromatography and Sephadex G-100 gel filtration. The final enzyme preparation had an activity of 2284 kininase U/E_<280>, which is the highest known among kininases derived from plants. This enzyme cleaved Gly^4-Phe^5 and Phe^5-Ser^6 bonds of the bradykinin molecule. Its molecular weight was estimated to be 6.7×10^4 and the optimum pH for the degradation of bradykinin was 8.0. The enzymatic activity of this enzyme was inhibited by mercurials, diisopropyl-fluorophosphate (DFP) and a high concentration of ethylenediaminetetraacetic acid (EDTA), but tosyllysine chloromethyl ketone (TLCK), tosylphenylalanine chloromethyl ketone (TPCK), iodoacetic acid, Trasylol and sodium tetrathionate had no detectable effect.
- 公益社団法人日本薬学会の論文
- 1982-06-25
著者
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木付 和幸
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Science University of Tokyo
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守屋 寛
Department of Biochemistry, Faculty of Pharmaceutical Sciences, Science University of Tokyo
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木付 和幸
山口東京理大 基礎工
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木付 和幸
Department Of Materials Science And Environmental Engineering Faculty Of Science And Engineering Tok
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守屋 寛
Department Of Biochemistry Faculty Of Pharmaceutical Sciences Science University Of Tokyo
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木付 和幸
山口東京理科大学、基礎工学部、物質・環境工学科
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