Studies in our laboratory have shown that the anion-sensitive Mg-ATPase is located in mitochondria, but not in the plasma membrane of rabbit gastric mucosa, trout gill, rabbit kidney and rat pancreas; whereas in rabbit erythrocyte membrane, it is part of the Ca-Mg activated ATPase system. These findings appear to rule out a function of the anion-sensitive ATPase in the transport of anions and protons across the plasma membrane in these tissues. On the other hand, the K-activated ATPase in a gradient-purified vesicle fraction of pig gastric mucosa mediates proton uptake in exchange for K+ in the presence of ATP, in agreement with earlier findings of other investigators. The enzyme requires a phospholipid environment for its activity. Studies of arginine modification with butanedione in the presence or absence of ATP and its analogues, and of activating cations indicate that the enzyme contains an essential arginine group involved in ATP binding; and that K+ induces a conformational change, which leads to decreased ATP binding and probably coincides with enzyme dephosphorylation. Similar studies of sulfhydryl modification with DTNB indicate that the enzyme contains an essential sulfhydryl group, which does not appear to be directly involved in ATP binding, but rather that ATP binding may induce a conformational change which makes the sulfhydryl group less accessible.