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Purification of bacterial membrane proteins |
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| Authors: | Charles Moldow John Robertson Lawrence Rothfield |
| Affiliation: | (1) Department of Microbiology, University of Connecticut Health Center, 06032 Farmington, Connecticut;(2) Present address: Department of Medicine, University of Minnesota Medical School, Minneapolis, Minnesota;(3) Present address: Applied Biochemistry Division, D.S.I.R. Private Bag, Palmerston North, New Zealand |
| Abstract: | Summary Guanidinium thiocyanate was shown to be effective in solubilizing over 80% of the protein of theE. coli cell envelope. Fractionation of the solubilized membrane polypeptides by ion exchange chromatography was achieved following removal of the guanidinium thiocyanate by dialysis against 6m urea. |
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