Properties of soluble ATPase from castor bean endosperm mitochondria

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概要

• 論文の詳細を見る

• An ATPase was extracted and purified from castor bean endosperm mitochondria. The enzyme is stable at 60℃ only in the presence of ATP in the incubation medium. It is less stable at 0℃ than at 30℃ but is stabilized by ammonium sulfate or glycerol. Activity is dependent on the presence of Mg^<++>, and in the presence of Mg^<++> is enhanced by 2,4-dinitrophenol, but. is not inhibited by oligomycin. The enzyme hydrolyzes ITP in addition to ATP, but ITPase activity is hardly enhanced by 2,4-dinitrophenol. This preparation has many properties in common with the ATPase (coupling factor 1) from beef heart mitochondria.

• 日本植物生理学会の論文

著者

• TAKEUCHI YASUAKI

  Department of Botany, Faculty of Science, University of Tokyo

• Yoshida Kunihisa

  Department Of Botany Faculty Of Science University Of Tokyo

• Takeuchi Yasuaki

  Department Of Botany Faculty Of Science University Of Tokyo

関連論文

• Electron transport dependent adenosine triphosphatase activity in castor bean endosperm mitochondria
• Properties of soluble ATPase from castor bean endosperm mitochondria

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