Purification and Properties of L-Arginine Decarboxylase of Evernia prunastri

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概要

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• An L-arginine decarboxylase was isolated from Evernia prunastri thallus. The enzyme was purified about 117-fold and showed a pH optimum of 7.1 and a temperature optimum at 26℃. Its molecular weight was estimated as 300,000. The Evernia arginine decarboxylase was significantly inhibited by L-ornithine, urea and putrescine. The K_m for L-arginine was about 12.5 mM.

• 日本植物生理学会の論文

著者

• Vicente Carlos

  Catedra De Fisiologia Vegetal Facultad De Biologia Universidad Complutense

• Legaz Estrella

  Catedra de Fisiologia Vegetal, Facultad de Biologia, Universidad Complutense

• Legaz Estrella

  Catedra De Fisiologia Vegetal Facultad De Biologia Universidad Complutense

関連論文

• Purification and Properties of L-Arginine Decarboxylase of Evernia prunastri

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