Beam K G, Alper S L, Palade G E, Greengard P
J Cell Biol. 1979 Oct;83(1):1-15. doi: 10.1083/jcb.83.1.1.
The catecholamine-stimulated cotransport of sodium and potassium ions across the plasma membrane of the turkey erythrocyte was previously found to be associated with increased 32P incorporation into a high molecular weight protein. To determine the subcellular localization of this phosphorylated protein, which we have termed goblin, a new method has been developed for isolation of pure plasma membranes from turkey erythrocytes. With this method, it has been demonstrated that goblin is located in the plasma membrane. Goblin is not extracted by solutions of low or high ionic strength but is partially extracted by nonionic detergents, indicating that it is not a component of turkey erythrocyte spectrin and suggesting that it may be an intrinsic protein of the plasma membrane. The data are compatible with a possible role for goblin in the hormonal control of ion movements across the plasma membrane.
先前发现，儿茶酚胺刺激的钠钾离子跨火鸡红细胞质膜的协同转运与32P掺入一种高分子量蛋白质的增加有关。为了确定这种我们称为“哥布林”的磷酸化蛋白的亚细胞定位，已开发出一种从火鸡红细胞中分离纯质膜的新方法。通过这种方法，已证明哥布林位于质膜中。哥布林不会被低离子强度或高离子强度的溶液提取，但会被非离子去污剂部分提取，这表明它不是火鸡红细胞血影蛋白的组成部分，并提示它可能是质膜的内在蛋白。这些数据与哥布林在激素控制离子跨质膜移动中可能发挥的作用相符。
