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Solubilization of the Cytoplasmic Membrane of <i>Escherichia coli</i> by the Ionic Detergent Sodium-Lauryl Sarcosinate

Journal of Bacteriology · 1973 · Vol. 115(3) · pp. 717–722

Camille C. Filip✉(The University of Texas at Austin)Gail Fletcher(The University of Texas at Austin)Judith L. Wulff(The University of Texas at Austin)Charles F. Earhart(The University of Texas at Austin)

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Abstract

The sensitivity of the outer and cytoplasmic membranes of Escherichia coli to detergent was examined by isopycnic sucrose density gradient centrifugation. Sodium lauryl sarcosinate (Sarkosyl) was found to disrupt the cytoplasmic membrane selectively under conditions in which Triton X-100 and dodecyl sodium sulfate solubilized all membrane protein. These results were verified by gel electrophoresis; membrane proteins solubilized by Sarkosyl were identical to those of the cytoplasmic membrane. The presence of Mg(2+) during treatment with Sarkosyl was found to afford partial protection of the cytoplasmic membrane from dissolution.

Enzyme Structure and Function Bacterial Genetics and Biotechnology Amino Acid Enzymes and MetabolismCytoplasmIsopycnicBiologyEscherichia coliSodium dodecyl sulfateDifferential centrifugationMembraneMembrane proteinSodiumCentrifugation

MeSH terms

Bacterial ProteinsCell FractionationCell MembraneCentrifugation, Density GradientElectrophoresis, Polyacrylamide GelEscherichia coliMagnesiumSarcosineSodium Dodecyl SulfateSolubilitySucroseSurface-Active Agents

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952

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