Partial characterization of a soluble ATPase from pea cotyledon mitochondria

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Abstract
A partially purified soluble ATPase (ATP phosphohydrolase, EC 3.6.1.3) from pea [Pisum sativum] cotyledon mitochondria was characterized. Inhibition patterns with azide, NaF, and cold, and a stimulation by 2,4-dinitrophenol were typical of F1-ATPases from mammalian mitochondria. The enzyme hydrolyzed GTP, ITP and ATP, but not CTP, UTP, ADP, or IDP. ATPase and ITPase activities were strongly inhibited by ADP and to a lesser extent by IDP. Distinctive properties of the pea mitochondrial enzyme were activation by high concentrations of CaCl2 and stimulation by NaCl.

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