Takeguchi N, Asano S, Morii M
Faculty of Pharmaceutical Sciences, Toyama Medical and Pharmaceutical University, Japan.
Nihon Rinsho. 1996 Mar;54(3):595-600.
Gastric H+, K+ -ATPase comprised of alpha- and beta-subunits was functionally expressed in an animal cell-line. When glutamic acid (345) of the alpha-subunit was mutated to glutamine, the affinity of K+ decreased 10-fold, indicating that this residue in the 4th transmembrane domain engages in the determination of the K+ affinity. The roles of other residues are also discussed. The number of the binding site of proton pump inhibitors such as omeprazole and E3810 (rabeprazole) is 1, which is contrary to the proposal of 2 or 3 by other researchers. The reason of this discrepancy is explained. The interaction between 2 or 4 alpha-subunits was shown to be necessary for the function of this pump. Finally, recent topics about H+ -ATPase are discussed.
由α亚基和β亚基组成的胃H⁺,K⁺ -ATP酶在一种动物细胞系中实现了功能表达。当α亚基的谷氨酸(345)突变为谷氨酰胺时,K⁺的亲和力下降了10倍,这表明第4个跨膜结构域中的这个残基参与了K⁺亲和力的决定。还讨论了其他残基的作用。奥美拉唑和E3810(雷贝拉唑)等质子泵抑制剂的结合位点数量为1,这与其他研究人员提出的2个或3个的观点相反。解释了这种差异的原因。已表明该泵的功能需要2个或4个α亚基之间的相互作用。最后,讨论了关于H⁺ -ATP酶的最新研究课题。