期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1977
卷号：74
期号：2
页码：529-532
DOI：10.1073/pnas.74.2.529
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：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.
