The molecular size required varies according to the reaction step round the sodium pump cycle

Progress along the path of the sodium pump cycle requires a stepwise recruitment of additional subunits for maximal activity. These results show that whereas a particle the size of the alpha beta protomer presents Na+,K+-ATPase activity at 10 microM ATP, an additional subunit, perhaps a second alpha-chain, is required to obtain the much greater Na+,K+-ATPase activity resulting from the occupation of low-affinity ATP sites at physiological ATP concentrations. A non-phosphorylating ATP analogue, however, will modestly stimulate the Na+,K+-ATPase activity acting at an alternative low-affinity site or step on the alpha beta protomer.