A SHORT POLYPEPTIDE MARKER SEQUENCE USEFUL FOR RECOMBINANT PROTEIN IDENTIFICATION AND PURIFICATION
A SHORT POLYPEPTIDE MARKER SEQUENCE USEFUL FOR RECOMBINANT PROTEIN IDENTIFICATION AND PURIFICATION
复制标题
DOI：
10.1038/nbt1088-1204
复制
发表时间：
1988-10-01
期刊：
影响因子：
--
通讯作者：
CONLON, PJ
中科院分区：
文献类型：
--
作者：
HOPP, TP;PRICKETT, KS;CONLON, PJ
将一个8个氨基酸的亲水性小肽（AspTyrLysAspAspAspAspAspLys）工程化到各种重组淋巴因子的N-末端，以帮助从酵母上清液或E.大肠杆菌提取物将对该序列的前四个氨基酸具有特异性的抗体用作检测试剂，并在温和条件下对产物进行免疫亲和纯化。由于肽部分的小尺寸及其亲水性，蛋白质不受其存在的影响，并保留了高水平的生物活性。此外，可以通过使用肠激酶的酶促切割程序去除肽。
A small hydrophilic peptide of eight amino acids (AspTyrLysAspAspAspAspLys) was engineered onto the N-terminus of a variety of recombinant lymphokines for the purpose of aiding in their detection and purification from yeast supernatants orE. coliextracts. An antibody specific for the first four amino acids of this sequence was used as a detection reagent and for immunoaffinity purification of products under mild conditions. Because of the small size of the peptide moiety and its hydrophilic nature, the proteins were unaffected by its presence and retained a high level of biological activity. In addition, it was possible to remove the peptide via an enzymatic cleavage procedure using enterokinase.