Helenius A, Simons K
Proc Natl Acad Sci U S A. 1977 Feb;74(2):529-32. doi: 10.1073/pnas.74.2.529.
Seventeen hydrophilic proteins and five amphiphilic membrane proteins were subjected to agarose gel electrophoresis in the presence of a nonionic detergent (Triton X-100), a mixture of anonionic and an anionic detergent (Triton X-100 and sodium deoxycholate), and a mixture of a nonionic and a cationic detergent (Triton X-100 and cetyltrimethylammonium bromide). The electrophoretic mobility of the hydrophilic proteins was unaffected in the three detergent mixtures. However, the mobility of the amphiphilic proteins shifted anodally in the Triton X-100-deoxycholate system and cathodally in the Triton X-100-cetyltrimethylammonium bromide system when compared to the mobility in Triton X-100 alone. The detergent-induced shift in mobility provides a simple, rapid, and sensitive method for distinguishing between hydrophilic and amphiphilic proteins.
17种亲水性蛋白质和5种两亲性膜蛋白在非离子去污剂(Triton X-100)、非离子与阴离子去污剂混合物(Triton X-100和脱氧胆酸钠)以及非离子与阳离子去污剂混合物(Triton X-100和十六烷基三甲基溴化铵)存在的情况下进行琼脂糖凝胶电泳。亲水性蛋白质在这三种去污剂混合物中的电泳迁移率未受影响。然而,与仅在Triton X-100中的迁移率相比,两亲性蛋白质的迁移率在Triton X-100 - 脱氧胆酸钠体系中向阳极移动,在Triton X-100 - 十六烷基三甲基溴化铵体系中向阴极移动。去污剂诱导的迁移率变化为区分亲水性蛋白质和两亲性蛋白质提供了一种简单、快速且灵敏的方法。