Patschinsky T, Walter G, Bister K
Virology. 1984 Jul 30;136(2):348-58. doi: 10.1016/0042-6822(84)90171-5.
Rabbit antisera were prepared against a synthetic peptide corresponding to the carboxyterminal amino acid sequences of the transforming protein p110gag-myc of avian oncovirus MC29. Analysis of immunoprecipitates formed with these sera (anti-mycC) demonstrated that the gag-myc hybrid proteins encoded by the avian leukemia viruses MC29, CMII, and OK10 were recognized by the anti-peptide sera, but not the gag or pol precursor proteins of helper viruses or the MH2-encoded p100gag-mil protein. In cells transformed by OK10 or MH2, putative v-myc proteins of 60K (OK10) and 59/61K (MH2) were also precipitated by anti-mycC. In addition, the anti-peptide sera reacted specifically with the gag-myc proteins encoded by three partially transformation-defective mutants of MC29, td10A, td10C, and td10H, and by MC29 variant HBI.
制备了兔抗血清,该抗血清针对与禽肿瘤病毒MC29的转化蛋白p110gag-myc的羧基末端氨基酸序列相对应的合成肽。对用这些血清(抗-mycC)形成的免疫沉淀物的分析表明,禽白血病病毒MC29、CMII和OK10编码的gag-myc杂合蛋白可被抗肽血清识别,但辅助病毒的gag或pol前体蛋白或MH2编码的p100gag-mil蛋白则不能被识别。在由OK10或MH2转化的细胞中,60K(OK10)和59/61K(MH2)的假定v-myc蛋白也可被抗-mycC沉淀。此外,抗肽血清与MC29的三个部分转化缺陷突变体td10A、td10C和td10H以及MC29变体HBI编码的gag-myc蛋白发生特异性反应。