Purification and Properties of L-Arginine Decarboxylase of Evernia prunastri |
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Authors: | Vicente Carlos; Legaz Estrella |
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Institution: | Cátedra de Fisiologia Vegetal, Facultad de Biologia, Universidad Complutense Madrid-3, Spain |
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Abstract: | An L-arginine decarboxylase was isolated from Evernia prunastrithallus. The enzyme was purified about 117-fold and showed apH optimum of 7.1 and a temperature optimum at 26°C. Itsmolecular weight was estimated as 300,000. The Evernia argininedecarboxylase was significantly inhibited by L-ornithine, ureaand putrescine. The Km for L-arginine was about 12.5 mM. (Received March 9, 1981; Accepted June 26, 1981) |
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