Hann S R, Abrams H D, Rohrschneider L R, Eisenman R N
Cell. 1983 Oct;34(3):789-98. doi: 10.1016/0092-8674(83)90535-4.
We have prepared an antiserum against a synthetic dodecapeptide whose sequence corresponds to the C terminus of the MC29 v-myc protein. This antiserum (anti-v-myc 12C) specifically precipitates the known gag-myc fusion proteins produced by the defective leukemia viruses MC29, CMII, and OK10, but does not react with gag-precursor or product proteins. In addition, proteins of 62 kd and 61/63 kd are precipitated by anti-v-myc 12C from OK10 and MH2 transformants, respectively. The serum also recognizes comigrating 62 kd proteins from three chicken bursal lymphoma cell lines and from the products of in vitro translation of c-myc-specific mRNA. All of these myc-related proteins are phosphorylated and all appear to be localized in the cell nucleus. In uninfected quail cells, anti-v-myc 12C also recognizes a candidate c-myc protein of 60 kd, which does not appear to be phosphorylated and is present in low levels relative to v-myc and lymphoma c-myc proteins.
我们制备了一种针对合成十二肽的抗血清，该十二肽的序列与MC29 v-myc蛋白的C末端相对应。这种抗血清（抗v-myc 12C）能特异性沉淀由缺陷型白血病病毒MC29、CMII和OK10产生的已知gag-myc融合蛋白，但不与gag前体蛋白或产物蛋白发生反应。此外，抗v-myc 12C分别从OK10和MH2转化体中沉淀出62 kd和61/63 kd的蛋白。该血清还能识别来自三种鸡法氏囊淋巴瘤细胞系以及c-myc特异性mRNA体外翻译产物中迁移率相同的62 kd蛋白。所有这些与myc相关的蛋白都被磷酸化，并且似乎都定位于细胞核中。在未感染的鹌鹑细胞中，抗v-myc 12C还能识别一种60 kd的候选c-myc蛋白，该蛋白似乎未被磷酸化，且相对于v-myc和淋巴瘤c-myc蛋白含量较低。
