Vassiliadou I, Leondiadis L, Ferderigos N, Ithakissios D S, Evangelatos G P, Livaniou E
Immunopeptide Chemistry Laboratory, Institute of Radioisotopes and Radiodiagnostic Products, NCSR Demokritos, Athens, Greece.
Peptides. 1999;20(3):411-4. doi: 10.1016/s0196-9781(98)00169-7.
We present here a study on the epitopic structure and the immunochemical characteristics of thymosin beta10 (Tbeta10), a 43 aminoacid peptide involved in important cellular mechanisms, by using the epitope mapping Multipin method. Octapeptides overlapping by one amino acid so as to represent the whole sequence of Tbeta10 were synthesized on polystyrene pins and screened, using an ELISA method, with a polyclonal antiserum raised against intact recombinant Tbeta10. The octapeptides were also tested with anti-peptide oligoclonal antisera raised against the synthetic fragments Tbeta10[1-16] and Tbeta10[31-43], with polyclonal antisera raised against natural thymosin gamma4 (Tbeta4) or thymosin beta9 (Tbeta9), and with anti-peptide oligoclonal antisera raised against various fragments of Tbeta4 (i.e. Tbeta4[1-11], Tbeta4[30-43] and Tbeta4[16-38]). Four distinct epitopic fragments were revealed, namely the sequences 1-13, 19-30, 29-40 and 36-43. Among them, the sequence 36-43 appears to offer unique immunochemical characteristics to the Tbeta10 molecule.
我们在此展示一项关于胸腺素β10（Tβ10）表位结构和免疫化学特性的研究，Tβ10是一种参与重要细胞机制的43个氨基酸的肽，采用表位作图多重针方法进行研究。在聚苯乙烯针上合成了彼此重叠一个氨基酸从而代表Tβ10完整序列的八肽，并使用酶联免疫吸附测定（ELISA）方法，用针对完整重组Tβ10产生的多克隆抗血清进行筛选。这些八肽还用针对合成片段Tβ10[1-16]和Tβ10[31-43]产生的抗肽寡克隆抗血清、针对天然胸腺素γ4（Tβ4）或胸腺素β9（Tβ9）产生的多克隆抗血清以及针对Tβ4各种片段（即Tβ4[1-11]、Tβ4[30-43]和Tβ4[16-38]）产生的抗肽寡克隆抗血清进行了检测。揭示了四个不同的表位片段，即序列1-13、19-30、29-40和36-43。其中，序列36-43似乎赋予Tβ10分子独特的免疫化学特性。
