Long C W, Berzinski T R, Gilden R V
Int J Cancer. 1977 Jun 15;19(6):843-50. doi: 10.1002/ijc.2910190616.
A low molecular weight, highly basic DNA-binding protein was purified from several oncornaviruses by the sequential procedures of gel filtration in guanidine-hydrochloride, DEAE-cellulose chromatography and affinity chromatography on single-stranded DNA sepharose. The binding protein from Rauscher and woolly monkey type-C viruses was the fastest migrating of the virion proteins in SDS-polyacrylamide gels and thus is designated p10 according to previous convention although our estimates of molecular weight were 8-9,000 daltons. The binding protein from these two viruses was resolved into two bands by acid-urea electrophoresis although only a single NH2 terminal amino acid was detected (S. Oroszlan, personal communication), thus indicating charge heterogeneity. Antibody to Rauscher virus p10 species-specific in gel diffusion and complement-fixation tests and did not exhibit cross-reactivity with other virion proteins. A DNA-binding protein was also detected in preparations of mouse mammary tumor virus. This purified protein had an apparent molecular weight of 12,500, was the second fastest migrating component in the virus preparations, and was antigenically unrelated to the mouse type-C virus p10.
通过在盐酸胍中进行凝胶过滤、DEAE-纤维素色谱以及在单链DNA琼脂糖上进行亲和色谱的连续步骤，从几种肿瘤病毒中纯化出一种低分子量、高碱性的DNA结合蛋白。劳舍尔病毒和绒毛猴C型病毒的结合蛋白在SDS-聚丙烯酰胺凝胶中是病毒粒子蛋白中迁移速度最快的，因此根据先前的惯例被命名为p10，尽管我们估计其分子量为8000 - 9000道尔顿。这两种病毒的结合蛋白通过酸性尿素电泳可分离成两条带，尽管只检测到一个NH2末端氨基酸（S.奥罗斯兰，个人交流），这表明存在电荷异质性。劳舍尔病毒p10的抗体在凝胶扩散和补体结合试验中具有种特异性，并且与其他病毒粒子蛋白没有交叉反应。在小鼠乳腺肿瘤病毒制剂中也检测到一种DNA结合蛋白。这种纯化蛋白的表观分子量为12500，是病毒制剂中迁移速度第二快的成分，并且在抗原性上与小鼠C型病毒p10无关。
