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Scherer GF. Auxin-stimulated ATPase in membrane fractions from pumpkin hypocotyls (Cucurbita maxima L.). Planta. 1981;151(5):434-8doi: 10.1007/BF00386536.
Scherer, G. F. (1981). Auxin-stimulated ATPase in membrane fractions from pumpkin hypocotyls (Cucurbita maxima L.). Planta, 151(5), 434-8. https://doi.org/10.1007/BF00386536
Scherer, G F. "Auxin-stimulated ATPase in membrane fractions from pumpkin hypocotyls (Cucurbita maxima L.)." Planta vol. 151,5 (1981): 434-8. doi: https://doi.org/10.1007/BF00386536
Scherer GF. Auxin-stimulated ATPase in membrane fractions from pumpkin hypocotyls (Cucurbita maxima L.). Planta. 1981 May;151(5):434-8. doi: 10.1007/BF00386536. PMID: 24302108.
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Planta. 1981 May;151(5):434-8. doi: 10.1007/BF00386536.

Auxin-stimulated ATPase in membrane fractions from pumpkin hypocotyls (Cucurbita maxima L.).

Planta

G F Scherer

Affiliations

  1. Botanisches Institut, Universität Bonn, Venusbergweg 22, D-5300, Bonn 1, Federal Republic of Germany.

PMID: 24302108 DOI: 10.1007/BF00386536

Abstract

Membrane fractions from Cucurbita maxima hypocotyls were isolated in a medium which inhibits the action of endogenous phospholipases. After removal of soluble phosphatases by Sepharose 2B-CL column chromatography, an auxin-stimulated ATPase activity was found in membrane fractions from linear sucrose gradients. In the presence of 10(-4) M phenylacetic acid (PAA), the stimulation by indol-3-acetic acid (IAA) exhibited a bimodal concentration dependence with maximal stimulation of about 50% at 10(-6) M IAA. Without PAA, only a high concentration of 10(-4) M IAA was stimulatory, whereas 10(-6) M IAA had no apparent effect and 10(-8) M IAA exhibited weak inhibition. PAA alone had only weak or no effects. The effects of IAA must be considered as hormone-specific. The ATPase activity in the presence of 10(-4) M PAA was activated only by 2,4-dichlorophenoxyacetic acid (2,4-D), an active auxin analogue, but not by the inactive stereoisomers, 2,3-D and 3,5-D. Comparison with marker enzyme profiles suggested that part of the auxin-stimulated ATPase was localized on plasma membranes as well as other compartments. Thus, the auxin-stimulated ATPase may become a useful tool in the investigation of the mechanism of action of auxin.

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