Properties of a soluble ATPase from castor bean endosperm mitochondria |
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Authors: | YOSHIDA KUNIHISA; TAKEUCHI YASUAKI |
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Institution: | Department of Botany, Faculty of Science, University of Tokyo Tokyo, Japan |
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Abstract: | An ATPase was extracted and purified from castor bean endospermmitochondria. The enzyme is stable at 60°C only in the presenceof ATP in the incubation medium. It is less stable at 0°Cthan at 30°C but is stabilized by ammonium sulfate or glycerol.Activity is dependent on the presence of Mg++, and in the presenceof Mg++ is enhanced by 2,4-dinitrophenol, but is not inhibitedby 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. (Received November 8, 1969; ) |
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