Abstract
ATPase activity of the plasma membrane fraction from primary roots of corn (Zea mays L. WF9 × M14) was activated by Mg2+ and further stimulated by monovalent cations (K+ > Rb+ > Cs+ > Na+ > Li+). K+-stimulated activity required Mg2+ and was substrate-specific. Maximum ATPase activity in the presence of Mg2+ and K+ was at pH 6.5 and 40 C. Calcium and lanthanum (<0.5 mm) were inhibitors of ATPase, but only in the presence of Mg2+. Oligomycin was not an inhibitor of the plasma membrane ATPase, whereas N,N′-dicyclohexylcarbodiimide was. Activity showed a simple Michaelis-Menten saturation with increasing ATP·Mg. The major effect of K+ in stimulating ATPase activity was on maximum velocity. The kinetic data of K+ stimulation were complex, but similar to the kinetics of short term K+ influx in corn roots. Both K+-ATPase and K+ influx kinetics met all criteria for negative cooperativity. The results provided further support for the concept that cation transport in plants is energized by ATP, and mediated by a cation-ATPase on the plasma membrane.
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Selected References
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