Brouwer J, Warnaar S O
J Gen Virol. 1980 Dec;51(Pt 2):409-14. doi: 10.1099/0022-1317-51-2-409.
Preparations of the 30 X 10(3) mol. wt. protein (p30) of Rauscher murine leukaemia virus (R-MuLV) which had been purified to homogeneity as judged by gel electrophoresis in the presence of SDS and by amino-terminal amino acid analysis, showed considerable isoelectric heterogeneity. It was found that R-MuLV p30 polypeptide chains are easily converted in vitro into chains with more acidic isoelectric points. R-MuLV p30 polypeptides with different isoelectric points displayed the same set of 125I-labelled tryptic peptides. It is concluded that the charge heterogeneity of R-MuLV p30, as revealed in isoelectric focusing experiments, is not caused by genetic heterogeneity of the virus genome but by post-translational modification.
劳氏鼠白血病病毒（R-MuLV）的30×10³分子量蛋白质（p30）制剂，经十二烷基硫酸钠存在下的凝胶电泳及氨基末端氨基酸分析判断已纯化至均一，显示出相当大的等电点不均一性。发现R-MuLV p30多肽链在体外容易转化为等电点更偏酸性的链。具有不同等电点的R-MuLV p30多肽显示出相同的一组¹²⁵I标记的胰蛋白酶肽段。得出的结论是，等电聚焦实验中揭示的R-MuLV p30的电荷不均一性不是由病毒基因组的遗传不均一性引起的，而是由翻译后修饰引起的。
