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The effect of auxin on membrane-bound ATPase activity was studied in a plasma membrane-enriched fraction from zucchini hypocotyls. The apparent KM of ATPase activity for ATP was decreased in the presence of 10-6 M auxin so that at very low ATP concentrations the stimulation of ATPase activity was most obvious. The weak auxin analogue, 2,3-dichlorophenoxyacetic acid, stimulated much less than the active auxin 2,4-dichlorophenoxyacetic acid.