Kinin-inactivating Enzyme from the Mushroom Tricholoma conglobatum. VI. Actions on Angiotensins I and II
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概要
- 論文の詳細を見る
A potent kinin-inactivating enzyme from the mushroom Tricholoma conglobatum, Shimeji kininase, liberated angiotensin II and the dipeptide, H-His-Leu-OH, from angiotensin I. Thus, this enzyme was considered to have both kininase and angiotensin I converting activities like kininase II (angiotensin I converting enzyme, EC 3.4.15.1), which is widely distributed in mammals of various species. On the other hand, this enzyme had angiotensinase activity in addition to angiotensin I converting activity. However, the rate of angiotensin II hydrolysis was very slow as compared with that of kinin hydrolysis ; the molar ratio of angiotensin II hydrolysis to bradykinin hydrolysis was about 1 : 70.
- 公益社団法人日本薬学会の論文
- 1981-09-25
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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