Abstract
An ATPase isolated from Pisum epicotyl which had previously been shown to be associated with plasma membrane [Planta, 146 (1979) 161], has been characterized with respect to substrate specificity, pH optima and ion stimulation. The enzyme exhibits a decided preference for ATP as a substrate and prefers slightly acidic pH values. It is activated by Mg 2+ or Mn 2+ but, unlike most other higher plant plasma membrane isolates, it is stimulated by monovalent anions rather than monovalent cations. Further, it exhibits an unusual inhibition by nitrate at high pH values.
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