反梯度聚丙烯酰胺凝胶电泳在十二烷基硫酸钠存在下能更好的分离蛋白质样品

M. Hashiguchi, K. Shimizu, T. Hashiguchi
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引用次数: 1

摘要

我们发现,在反梯度(15-5%)凝胶上存在十二烷基硫酸钠的聚丙烯酰胺凝胶电泳中,蛋白质的分子质量与其迁移率之间的关系在双对数图上是线性的。相比之下,对于在10%的标准凝胶上溶解的蛋白质,这种关系不是线性的,而是符合两条直线。两种凝胶类型在分离小于100 kDa的蛋白质时具有相似的斜率,但反梯度(15-5%)凝胶分离分子质量范围更广的蛋白质。另一方面,10%的标准凝胶可以更好地分离大于100 kDa的蛋白质。这些结果表明,15-5%的反梯度凝胶最适合分离小于100 kDa的蛋白质。反梯度凝胶SDS-PAGE的优势可能源于反梯度凝胶中sds -蛋白复合物的解层速度比标准10%凝胶更快、更完全。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Inverse-gradient polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate for better separation of protein samples
We found that the relationship between the molecular mass of a protein and its mobility in polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate on an inverse-gradient (15-5%) gel is linear on a double logarithmic plot. In contrast, this relationship is not linear for proteins resolved on a standard 10% gel, but is fitted to two straight lines. Both gel types gave a similar slope in resolving proteins smaller than 100 kDa but inverse-gradient (15-5%) gel separated proteins with wider range of molecular mass. On the other hand, the standard 10% gel provided better separation of proteins larger than 100 kDa. These results suggest that the 15-5% inverse-gradient gel is best suited for the separation of proteins smaller than 100 kDa. The advantage of inverse-gradient gel SDS-PAGE may stem from the fact that unstacking of SDS-protein complexes in inverse-gradient gels is faster and more complete than in standard 10% gels.
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