Kinin Inactivating Enzyme from Mushroom Tricholoma conglobatum. I. Purification and the Sites of Action on Bradykinin Molecule
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概要
- 論文の詳細を見る
Potent kininase activities were found in Japanese mushrooms. Especially Tricholoma conglobatum (shimeji, in Japanese) contained 40-334 kininase units/g and the enzyme was purified by water extraction, ammonium sulfate fractionation, diethylaminoethyl (DEAE)-Sephadex A-50 chromatography and Sephadex G-100 gel filtration. The final preparation gave a single band in disc electrophoresis and its kininase activity, that was expressed in terms of μg bradykinin degraded in 1 min at 30°, was 480 units/E_280. This value was extremely potent, so this enzyme could be expected as a useful agent on the clinical purposes or other investigations of kallikrein-kinin system. The sites of action of this enzyme on bradykinin molecule were investigated by examination of 1-dimethylaminonaphthalene-5-sulphonyl (DNS)-modified products, which were liberated from bradykinin by this enzyme, on thin layer chromatography. It cleaved Gly^4-Phe^5 and Pro^7-Phe^8 bonds and the former bond was split more easily than the latter one.
- 社団法人日本薬学会の論文
- 1976-08-25
著者
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木付 和幸
山口東京理大 基礎工
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森脇 千秋
Laboratory Of Physiological Chemistry Faculty Of Pharmaceutical Sciences Science University Of Tokyo
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木付 和幸
Laboratory of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Science University of Tok
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守屋 寛
Laboratory of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Science University of Tok
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法島 義男
Laboratory of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Science University of Tok
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法島 義男
Faculty Of Pharmaceutical Sciences Science University Of Tokyo:(present Address)department Of Immuno
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森脇 千秋
Laboratory of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Science University of Tokyo
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