Gastric H/K-ATPase liberates two moles of Pi from one mole of phosphoenzyme formed from a high-affinity ATP binding site and one mole of enzyme-bound ATP at the low affinity site during cross-talk between catalytic subunits.
Gastric H/K-ATPase liberates two moles of Pi from one mole of phosphoenzyme formed from a high-affinity ATP binding site and one mole of enzyme-bound ATP at the low affinity site during cross-talk between catalytic subunits.
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在催化亚基之间的串扰过程中，胃 H/K-ATP 酶从高亲和力 ATP 结合位点形成的 1 摩尔磷酸酶和低亲和力位点处的 1 摩尔酶结合 ATP 中释放出 2 摩尔 Pi。
DOI：
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发表时间：
2002
期刊：
影响因子：
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通讯作者：
K.Abe
中科院分区：
文献类型：
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作者：
Watanabe T;Horiuchi T.;K.Abe
