Kinin inactivating enzyme from mushroom Tricholoma conglobatum. I. Purification and the sites of action on bradykinin molecule.

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Abstract
T. 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 .mu.g bradykinin degraded in 1 min at 30.degree., was 480 units/E280. This value was extremely potent, so this enzyme could be a useful agent for clinical purposes or other investigations of kallikrein-kinin system. The sites of action of this enzyme on the bradykinin molecule were investigated by examination of 1-dimethylaminonaphthalene-5-sulfonyl (DNS)-modified products, which were liberated from bradykinin by this enzyme, on TLC. It cleaved Gly4-Phe5 and Pro7-Phe8 bonds and the former bond was split more easily than the latter one.

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