Avruch J, Fairbanks G
Proc Natl Acad Sci U S A. 1972 May;69(5):1216-20. doi: 10.1073/pnas.69.5.1216.
Human erythrocyte membranes are phosphorylated by [gamma-(32)P]ATP in association with the Mg(++)-dependent, Na(+) and K(+)-stimulated ATPase (EC 3.1.6.3) reaction. To delineate the membrane species involved, phosphorylated membranes were analyzed by polyacrylamide gel electrophoresis in sodium dodecyl sulfate, under conditions that minimize hydrolysis of acyl phosphate linkages. Three radioactive components were detected, of which only one was a phosphopeptide, of apparent molecular weight 105,000. The phosphate bound to this peptide undergoes rapid turnover and is discharged by hydroxylamine. In the presence of Mg(++), the phosphorylation of this peptide is specifically stimulated by Na(+) and blocked by ethylene diamine tetraacetate; its dephosphorylation is stimulated by K(+) and blocked by ouabain. We conclude that this phosphopeptide is an intermediate in the Mg(++)-dependent, Na(+)- and K(+)-stimulated ATPase reaction of the erythrocyte membrane.
人红细胞膜在与镁离子依赖的、钠钾刺激的ATP酶（EC 3.1.6.3）反应相关的过程中被[γ-(32)P]ATP磷酸化。为了确定所涉及的膜成分，在使酰基磷酸键水解最小化的条件下，通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳对磷酸化膜进行分析。检测到三种放射性成分，其中只有一种是磷酸肽，表观分子量为105,000。与该肽结合的磷酸盐经历快速周转并被羟胺释放。在镁离子存在下，该肽的磷酸化被钠离子特异性刺激并被乙二胺四乙酸阻断；其去磷酸化被钾离子刺激并被哇巴因阻断。我们得出结论，这种磷酸肽是红细胞膜镁离子依赖的、钠钾刺激的ATP酶反应中的一个中间体。
