Renaud M, Fasiolo F, Baltzinger M, Boulanger Y, Remy P
Eur J Biochem. 1982 Apr 1;123(2):267-74. doi: 10.1111/j.1432-1033.1982.tb19763.x.
Yeast phenylalanyl-tRNA synthetase was specifically labelled with a 3'-oxidised tRNAPhe. Stoichiometric inactivation was achieved with the incorporation of 2 mol oxidised tRNA Phe/mol enzyme which corresponds exactly to the stoichiometry of tRNA binding. The labelled peptide has been isolated using a quick chromatographic procedure which can be applied to any covalent complex formed between a tRNA and an aminoacyl tRNA synthetase. The isolated peptide (18 amino acids) was found to encompass the unique cysteine sequence of the smaller beta subunit of the enzyme.
酵母苯丙氨酰 - tRNA合成酶用3'-氧化的tRNAPhe进行了特异性标记。通过每摩尔酶掺入2摩尔氧化的tRNAPhe实现了化学计量失活，这与tRNA结合的化学计量完全一致。使用一种快速色谱方法分离出了标记的肽段，该方法可应用于tRNA与氨酰 - tRNA合成酶之间形成的任何共价复合物。发现分离出的肽段（18个氨基酸）包含该酶较小的β亚基独特的半胱氨酸序列。
