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Plant Physiology 65:1085-1089 (1980)
© 1980 American Society of Plant Biologists

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Articles

Electrical Evidence for Different Mechanisms of Uptake for Basic, Neutral, and Acidic Amino Acids in Oat Coleoptiles 1,2

Thomas B. Kinraide and Bud Etherton

Department of Botany, University of Vermont, Burlington, Vermont 05405

The application of neutral or acidic amino acids to oat coleptiles induced transient depolarizations of the membrane potentials. The depolarizations are considered to reflect H+ -amino acid co-transport, and the spontaneous repolarizations are believed to be caused by subsequent electrogenic H+ extrusion. The basic amino acids depolarized the cell membrane strongly, but the repolarizations were weak or absent. The depolarizations induced by the basic amino acids were weakly sensitive to manipulations of the extracellular and intracellular pH. The depolarizations induced by the other amino acids, in contrast, were more strongly affected by the pH changes. Several amino acids induced distinct but diminished depolarizations in the presence of 2,4-dinitrophenol or cyanide, but the repolarizations were generally eliminated. These experiments support the co-transport theory but suggest somewhat different mechanisms for the transport of the neutral, acidic, and basic amino acids. We suggest that the neutral amino acids are co-transported with a single H+ and that accumulation depends upon both the {Delta}pH and the membrane potential components of the proton motive force. The acidic amino acids appear to be accumulated by a similar mechanism except that the transport of each molecule may be associated with a cation in addition to a single proton. The permanently protonated basic amino acids appear not to be co-transported with an additional proton. Accumulation would depend only on the membrane potential component of the proton motive force.


1 Research supported in part by National Science Foundation Grant PCM78-22826 and by the Vermont Agricultural Experiment Station.

2 Vermont Agricultural Experiment Station Journal Article No. 431.




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