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• W2046864902 abstract "Despite the importance of membranes in any living system, the global analysis of membrane subproteomes is still a common obstacle. In particular, the widely used 2-DE technique consisting of IEF in the first dimension and SDS-PAGE in the second dimension has some major drawbacks regarding the separation of hydrophobic proteins. Therefore, we applied an alternative electrophoretic technique for separating membrane proteins: two-dimensional BAC/SDS electrophoresis (2-DB) using the cationic detergent benzyldimethyl-n-hexadecylammonium chloride in the first and the anionic detergent SDS in the second dimension. The use of 2-DB resulted in an improved separation of hydrophobic proteins. Thus, extremely hydrophobic proteins such as cytochrome-c oxidase subunit I with a grand average hydrophobicity (GRAVY) index of 0.74 and a total of 12 known transmembrane domains (TMD) or Sec61α with a GRAVY index of 0.56 and a total of ten known TMD could be identified by MS/MS analyses of protein spots derived from 2-DB gels." @default.
• W2046864902 created "2016-06-24" @default.
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• W2046864902 date "2005-09-01" @default.
• W2046864902 modified "2023-10-18" @default.
• W2046864902 title "Two-dimensional benzyldimethyl-n-hexadecylammonium chloride/SDS-PAGE for membrane proteomics" @default.
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• W2046864902 doi "https://doi.org/10.1002/pmic.200401214" @default.
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