Ferro-Luzzi Ames G, Nikaido K
Eur J Biochem. 1981 Apr;115(3):525-31.
The pattern of post-translational protein modifications involving a phosphate group was determined in the prokaryotes Salmonella typhimurium and Escherichia coli. A special two-dimensional gel electrophoretic separation was developed which utilizes acidic urea in the first dimension and neutral sodium dodecyl sulfate in the second dimension. This system allows survival and visualization of a number of proteins which are otherwise lost in systems employing basic conditions. The total number of phosphate-containing proteins thus obtained is approximately twenty. Among them are included proteins containing nucleotidylyl groups; two of these have been identified: glutamine synthetase (adenylylated) and regulatory protein PII (uridylylated). Two phosphate-containing proteins are shown to be regulated by the level of K+. The pattern of phosphorylation is shown to change with changing growth conditions and with specific mutations.
在鼠伤寒沙门氏菌和大肠杆菌这两种原核生物中，确定了涉及磷酸基团的翻译后蛋白质修饰模式。开发了一种特殊的二维凝胶电泳分离方法，该方法在第一维使用酸性尿素，在第二维使用中性十二烷基硫酸钠。该系统能使许多在使用碱性条件的系统中会丢失的蛋白质得以保留并可视化。由此获得的含磷蛋白质总数约为二十种。其中包括含核苷酸基团的蛋白质；已鉴定出其中两种：谷氨酰胺合成酶（腺苷酸化）和调节蛋白PII（尿苷酸化）。两种含磷蛋白质显示受钾离子水平调节。磷酸化模式显示会随着生长条件的变化和特定突变而改变。
