In vitro stimulation by 2,4-dichlorophenoxyacetic acid of an ATPase and inhibition of phosphatidate phosphatase of plant membranes

Scherer, G.F.; Morré, D.J.

Biochemical and Biophysical Research Communications 84(1): 238-247

1978


ISSN/ISBN: 0006-291X
PMID: 215139
DOI: 10.1016/0006-291x(78)90288-7
Accession: 068524353

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Abstract
The auxin herbicide 2,4-D was shown to modulate the activities of several phosphatases with membranes isolated from soybean hypocotyls under conditions where degradative changes in the membranes were minimized. The medium for isolaton of membranes consisted of 0.1 M Tris/HCl or Tris/acetate, pH 6.5, 0.5 M sucrose, 4% choline (wt/wt) and 4% ethanolamine (vol/vol) to inhibit phospholipase D, 20 mM EGTA [ethyleneglycol-bis-(.beta. aminoethyl ether) N,N-tetracetic acid] and 1 mM nupercaine, to inhibit phospholipase A. The inactive auxin analog 2,3-D, did not influence ATPase activity. Endogenous release of inorganic phosphate from an unidentified source was also stimulated 30% by 2,4-D. Phosphatidate phosphatase was inhibited by 2,4-D, whereas hydrolysis of G-6-P was not influenced by 2,4-D under the same conditions. These observations may be of relevance to the proton pump hypothesis of growth regulation.