The effect of external Na plus concentration on the transport of K plus was studied using K plus-depleted cells of a marine pseudomonad. K plus transport was found to be a saturable process and requires Na plus. The initial rates for K plus transport over a range of external K plus concentrations were measured in suspensions containing various fixed concentrations of Na plus. Reciprocals of the initial rates for K plus transport were plotted against reciprocals of the external concentration of K plus or Na plus to yield two primary Lineweaver-Burk plots. The experimental data were found to fit bisubstrate enzyme kinetics, with a sequential type mechanism. However, the initial rate data did not allow distinction between ordered or random mechanisms. The results suggest that Na plus and K plus form a ternary complex with a specific K plus carrier molecule on the outer surface of the membrane prior to translocation and the release of K plus inside the cell.
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