Ohba M, Koiwai O, Tanada S, Hayashi H
J Biochem. 1979 Nov;86(5):1233-8. doi: 10.1093/oxfordjournals.jbchem.a132638.
A protein existing mainly in the supernatant fraction of Escherichia coli was found to be methylated by accepting the methyl moiety originating from methionine. The protein was identified as peptide synthesis elongation factor Tu (EF-Tu) by the following criteria. 1) The methylatable protein separated at the same position as purified EF-Tu on two-dimensional gel electrophoresis. 2) The methylatable protein interacted with antiserum specific for EF-Tu. Amino acid analysis of the methyl-labeled protein suggested that the site of methylation was an epsilon-amino group of lysine.
发现一种主要存在于大肠杆菌上清液部分的蛋白质通过接受来自甲硫氨酸的甲基部分而发生甲基化。通过以下标准将该蛋白质鉴定为肽合成延伸因子Tu(EF-Tu)。1)在二维凝胶电泳中,可甲基化的蛋白质与纯化的EF-Tu在相同位置分离。2)可甲基化的蛋白质与针对EF-Tu的抗血清相互作用。对甲基标记蛋白质的氨基酸分析表明,甲基化位点是赖氨酸的ε-氨基。