Perucho M, Salas J, Salas M L
Eur J Biochem. 1977 Dec;81(3):557-62. doi: 10.1111/j.1432-1033.1977.tb11982.x.
The DNA-binding protein P8 from transformed hamster fibroblasts (line NIL-1-hamster sarcoma virus) has been purified to homogeneity by DNA-cellulose and phosphocellulose chromatography. The molecular weight of dissociated P8 is 36000, the same as that reported for the subunits of glyceraldehyde-3-phosphate dehydrogenase, and the mobility of these proteins in polyacrylamide gels is identical. The amino acid composition of P8 is very similar to that of glyceraldehyde-3-phosphate dehydrogenase. When assayed for glyceraldehyde-3-phosphate dehydrogenase activity the P8 preparation had a specific activity of 54.6 units/mg, a value comparable to that of the crystalline enzyme from several sources. Furthermore, serum prepared against P8 crossreacts with glyceraldehyde-3-phosphate dehydrogenase from hamster muscle. These results show that P8 is glyceraldehyde-3-phosphate dehydrogenase. The interaction of P8 from transformed fibroblasts and glyceraldehyde-3-phosphate dehydrogenase from hamster and rabbit muscle with DNA has been studied using a Millipore filtration technique. These proteins have affinity for single-stranded DNA but not for double-stranded DNA.
来自转化的仓鼠成纤维细胞（NIL - 1 - 仓鼠肉瘤病毒株）的DNA结合蛋白P8已通过DNA - 纤维素和磷酸纤维素色谱法纯化至同质。解离后的P8分子量为36000，与磷酸甘油醛脱氢酶亚基的报道分子量相同，并且这些蛋白质在聚丙烯酰胺凝胶中的迁移率相同。P8的氨基酸组成与磷酸甘油醛脱氢酶非常相似。在检测磷酸甘油醛脱氢酶活性时，P8制剂的比活性为54.6单位/毫克，该值与来自多个来源的结晶酶相当。此外，针对P8制备的血清与仓鼠肌肉中的磷酸甘油醛脱氢酶发生交叉反应。这些结果表明P8是磷酸甘油醛脱氢酶。使用微孔过滤技术研究了来自转化成纤维细胞的P8与仓鼠和兔肌肉中的磷酸甘油醛脱氢酶与DNA的相互作用。这些蛋白质对单链DNA有亲和力，但对双链DNA没有亲和力。
