Na,K-ATPase, an integral protein of the plasma membrane of eukaryotic cells, derives energy from ATP hydrolysis for the active, coupled transport of Na+ out of the cell and K+ into the cell. The enzyme can be purified in membrane-associated form (1). It consists of two polypeptide chains: α(Mr=100,000) and β(Mr=50-60,000).Two dimensional arrays of the enzyme were induced by partial removal of its phospholipids by phospholipase A2, and in the presence of variousions. The arrays were exclusively dimeric with an (αβ)2 structure in the unit cell (Fig. 1). SDS polyacrylamide gel of the crystalline sheets is presented in Fig. 2. It shows an identical pattern with the same relative ratio of α:β subunits, to that of the pure enzyme.
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