Hosey M M, Plut D A, Tao M
Biochim Biophys Acta. 1978 Jan 19;506(2):211-20. doi: 10.1016/0005-2736(78)90392-9.
This report presents studies on the effect of diamide on protein phosphorylation in erythrocyte membranes. Diamide, a thiol-oxidizing reagent, nonspecifically inhibits cyclic Amp-dependent and -independent autophosphorylation of red cell memvranes, but not the activity of the solubilized membrane cycle AMP-independent protein kinases. Analysis of diamide-treated membranes by gel electrophoresis indicates that diamide is capable of inducing cross-linking of membrane proteins. The action of diamide, both in the inhibition of membrane autophosphorylation and in the cross-linking of membrane proteins, is very similar to that of Cu2+. o-phenanthroline complex. Our data indicate that diamide inhibits erythrocyte membrane autophosphorylation by perturbing the protein substrates.
本报告介绍了关于二酰胺对红细胞膜中蛋白质磷酸化作用的研究。二酰胺是一种硫醇氧化试剂，它非特异性地抑制红细胞膜中依赖和不依赖环磷酸腺苷（cAMP）的自磷酸化，但不影响可溶性膜中不依赖cAMP的蛋白激酶的活性。通过凝胶电泳对经二酰胺处理的膜进行分析表明，二酰胺能够诱导膜蛋白交联。二酰胺在抑制膜自磷酸化和膜蛋白交联方面的作用，与铜离子邻菲罗啉络合物的作用非常相似。我们的数据表明，二酰胺通过干扰蛋白质底物来抑制红细胞膜自磷酸化。
