Chemical and Pharmaceutical Bulletin
Online ISSN : 1347-5223
Print ISSN : 0009-2363
ISSN-L : 0009-2363
Kinin Inactivating Enzyme from Mushroom Tricholoma conglobatum. I. Purification and the Sites of Action on Bradykinin Molecule
木付 和幸森脇 千秋法島 義男守屋 寛
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1976 年 24 巻 8 号 p. 1742-1748

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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/E280. 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 Gly4-Phe5 and Pro7-Phe8 bonds and the former bond was split more easily than the latter one.
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© The Pharmaceutical Society of Japan
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