期刊
PROTEOMICS
卷 4, 期 9, 页码 2567-2571出版社
WILEY
DOI: 10.1002/pmic.200400829
关键词
doubled sodium dodecyl sulfate-polyacrylamide gel electrophoresis; mass spectrometry; membrane proteins; silver-stain
Acrylamide concentration, urea content, and the trailing ion used for sodium dodecyl sulfate (SDS)-gels modify electrophoretic protein mobilities in a protein-dependent way. Varying these parameters we coupled two SDS-gels to a two-dimensional (2-D) electrophoresis system. Protein spots in 2-D gels are dispersed around a diagonal. Hydrophobic proteins are well separated from water-soluble proteins which is the essential advantage of the novel technique. Mass spectrometric identification of previously unaccessible hydrophobic proteins is now possible.
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