Mulherkar R, Saraf A, Wagle A, Deo M G
FEBS Lett. 1986 Oct 20;207(1):142-4. doi: 10.1016/0014-5793(86)80028-x.
A unique polypeptide, called enhancing factor (EF), which enhances the binding of labeled epidermal growth factor (EGF) to cells, has been isolated. It has been purified to homogeneity from the acid-soluble proteins of mouse intestines. Earlier, EF was partially purified by two cycles of gel-permeation chromatography on Bio-Gel columns. We now report the final purification of EF on high-performance liquid chromatography (HPLC), using a reverse-phase column (mu Bondapak C18). The purity of the protein was confirmed when a single peak was obtained in HPLC. Also, a single protein band was obtained in SDS-PAGE. Purified EF has the same properties in vitro as those reported earlier for partially purified EF.
一种名为增强因子(EF)的独特多肽已被分离出来,它能增强标记的表皮生长因子(EGF)与细胞的结合。它已从小鼠肠道的酸溶性蛋白中纯化至同质。此前,EF通过在Bio-Gel柱上进行两轮凝胶渗透色谱进行了部分纯化。我们现在报告使用反相柱(μBondapak C18)在高效液相色谱(HPLC)上对EF进行最终纯化。当在HPLC中获得单个峰时,证实了该蛋白质的纯度。此外,在SDS-PAGE中获得了单一蛋白条带。纯化后的EF在体外具有与早期报道的部分纯化的EF相同的性质。