Direct Evidence for In Vivo Reversible Tyrosine Phosphorylation c the N-Terminal Domain of the H/K-ATPase a-Subunit in Mammali; Stomach Cells

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In vivo reversible phosphorylation of Tyr-7 and Tyr-10 of the pig stomach H/K-ATPase alpha-chain was initially demonstrated in mammals, rat, rabbit, and pig, in the presence of vanadate + H(2)O(2). In vitro phosphorylation has also been unequivocally demonstrated via the use of protease inhibitors during membrane H/K-ATPase preparation. An amphoretic detergent permitted each intrinsic kinase to phosphorylate each fusion protein containing the requisite Tyr residues, along with a reduction in alpha-chain phosphorylation. These and other data suggest that some important enzyme systems are present in the apical membrane and that they are in sufficient proximity to participate in the reversible phosphorylation of the amino terminal soluble domain of the alpha-chain with an unknown physiological function in the membrane embedded H/K-ATPase.

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