Different approaches to the mechanism of the sodium pump

The way in which the sodium pump uses energy from the hydrolysis of ATP to perform osmotic and electrical work is not yet understood. We attempt to bring together the results of a number of different approaches to this problem. One approach has been to correlate biochemical changes and ionic fluxes, both when the pump operates normally and when it operates in various abnormal 'modes' in particular unphysiological conditions. A second approach has been to expose fragments of cell membrane to (gamma-32P)ATP and to study the properties of components of the membrane that become labelled. It is now clear that 32P can be transferred to the beta-carboxy group of an aspartyl residue in a pump polypeptide, but there is controversy about the interrelations of different forms of this polypeptide and its role, if any, in the normal functioning of the pump. A third approach has been to attempt to purify the pump and to determine the properties of the pure enzyme. It seems that the pump contains a polypeptide (molecular weight about 100,000), which bears the phosphorylation site, and a smaller glycopeptide, but there is disagreement about the molecular ratios. The results of these and other approaches cannot yet be fitted into a satisfactory model for the sodium pump, but we shall consider some of the problems involved in this task.