Biochemical Pharmacology volume 78, issue 8, P1069-1074 2009 DOI: 10.1016/j.bcp.2009.06.007 View full text
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Hideo Ochiai, Kazuo Takeda, Shiori Soeda, Yoshikazu Tahara, Hitoshi Takenaka, Kazuhiro Abe, Yutaro Hayashi, Shunsuke Noguchi, Masumi Inoue, Silvia Schwarz, Wolfgang Schwarz, Masaru Kawamura

Abstract: Four catechins, epigallocatechin-3-gallate, epigallocatechin, epicatechin-3-gallate, and epicatechin, inhibited activity of the Na(+),K(+)-ATPase. The two galloyl-type catechins were more potent inhibitors, with IC(50) values of about 1 microM, than were the other two catechins. Inhibition by epigallocatechin-3-gallate was noncompetitive with respect to ATP. Epigallocatechin-3-gallate reduced the affinity of vanadate, shifted the equilibrium of E1P and E2P toward E(1)P, and reduced the rate of the E1P to E2P t…

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