DOI: 10.1128/jb.108.1.545-552.1971. Solubilization of the Cytoplasmic Membrane of <i>Escherichia coli</i> by Triton X-100

Solubilization of the Cytoplasmic Membrane of Escherichia coli by Triton X-100

10.1128/jb.108.1.545-552.1971

Crossref journal-article

American Society for Microbiology

Journal of Bacteriology (235)

Abstract

Treatment of a partially purified preparation of cell walls of Escherichia coli with Triton X-100 at 23 C resulted in a solubilization of 15 to 25% of the protein. Examination of the Triton-insoluble material by electron microscopy indicated that the characteristic morphology of the cell wall was not affected by the Triton extraction. Contaminating fragments of the cytoplasmic membrane were removed by Triton X-100, including the fragments of the cytoplasmic membrane which were normally observed attached to the cell wall. Treatment of a partially purified cytoplasmic membrane fraction with Triton X-100 resulted in the solubilization of 60 to 80% of the protein of this fraction. Comparison of the Triton-soluble and Triton-insoluble proteins from the cell wall and cytoplasmic membrane fractions by polyacrylamide gel electrophoresis after removal of the Triton by gel filtration in acidified dimethyl formamide indicated that the detergent specifically solubilized proteins of the cytoplasmic membrane. The proteins solubilized from the cell wall fraction were qualitatively identical to those solubilized from the cytoplasmic membrane fraction, but were present in different proportions, suggesting that the fragments of cytoplasmic membrane which are attached to the cell wall are different in composition from the remainder of the cytoplasmic membrane of the cell. Treatment of unfractionated envelope preparations with Triton X-100 resulted in the solubilization of 40% of the protein, and only proteins of the cytoplasmic membrane were solubilized. Extraction with Triton thus provides a rapid and specific means of separating the proteins of the cell wall and cytoplasmic membrane of E. coli .

Bibliography

Schnaitman, C. A. (1971). Solubilization of the Cytoplasmic Membrane of Escherichia coli by Triton X-100. Journal of Bacteriology, 108(1), 545â552.

Authors 1

Carl A. Schnaitman (first)

References 9 Referenced 432

Bayer , M. E. 1968 . Areas of adhesion between the wall and membrane of Escherichia coli . J. Gen. Microbiol. 53 : 395 - 404 . (10.1099/00221287-53-3-395) / J. Gen. Microbiol. / Areas of adhesion between the wall and membrane of Escherichia coli by Bayer M. E. (1968)
Bayer M. E. and C. C. Remsen. 1970. Structure of Esche-J. BACTERIOL.
Birdsell , D. C. , and E. H. Cota-Robles . 1968 . Lysis of spheroplasts of E. coli by a non-ionic detergent . Biochem. Biophys. Res. Commun. 31 : 438 - 446 . (10.1016/0006-291X(68)90496-8) / Biochem. Biophys. Res. Commun. / Lysis of spheroplasts of E. coli by a non-ionic detergent by Birdsell D. C. (1968)
Cota-Robles , E. H. 1963 . Electron microscopy of plasmolysis in Escherichia coli . J. Bacteriol. 85 : 499 - 503 . (10.1128/jb.85.3.499-503.1963) / J. Bacteriol. / Electron microscopy of plasmolysis in Escherichia coli by Cota-Robles E. H. (1963)
DePamphilis , M. L. , and J. Adler . 1971 . Attachment of flagellar basal bodies to the cell envelope: specific attachment to the outer lipopolysaccharide membrane and the cytoplasmic membrane . J. Bacteriol. 105 : 396 - 407 . (10.1128/JB.105.1.396-407.1971) / J. Bacteriol. / Attachment of flagellar basal bodies to the cell envelope: specific attachment to the outer lipopolysaccharide membrane and the cytoplasmic membrane by DePamphilis M. L. (1971)
Fox , C. F. , and E. P. Kennedy . 1965 . Specific labeling and partial purification of the m protein, a component of the ,i-galactoside transport system of Escherichia coli . Proc. Nat. Acad. Sci. U.S.A. 54 : 891 - 899 . (10.1073/pnas.54.3.891) / Proc. Nat. Acad. Sci. U.S.A. / Specific labeling and partial purification of the m protein, a component of the ,i-galactoside transport system of Escherichia coli by Fox C. F. (1965)
Schnaitman , C. A. 1970 . Examination of the protein composition of the cell envelope of Escherichia coli by polyacrylamide gel electrophoresis . J. Bacteriol. 104 : 882 - 889 . (10.1128/jb.104.2.882-889.1970) / J. Bacteriol. / Examination of the protein composition of the cell envelope of Escherichia coli by polyacrylamide gel electrophoresis by Schnaitman C. A. (1970)
Schnaitman , C. A. 1970 . Protein composition of the cell wall and cytoplasmic membrane of Escherichia coli . J. Bacteriol. 104 : 890 - 901 . (10.1128/jb.104.2.890-901.1970) / J. Bacteriol. / Protein composition of the cell wall and cytoplasmic membrane of Escherichia coli by Schnaitman C. A. (1970)
Schnaitman , C. A. 1971 . Effect of ethylenediaminetetraacetic acid, Triton X-100, and Iysozyme on the morphology and chemical composition of the cell wall of Escherichia coli . J Bacteriol. 108 : 553 - 563 . (10.1128/JB.108.1.553-563.1971) / J Bacteriol. / Effect of ethylenediaminetetraacetic acid, Triton X-100, and Iysozyme on the morphology and chemical composition of the cell wall of Escherichia coli by Schnaitman C. A. (1971)

Dates

Type	When
Created	5 years, 7 months ago (Jan. 3, 2020, 8:38 a.m.)
Deposited	4 years, 1 month ago (July 29, 2021, 1 p.m.)
Indexed	4 days, 13 hours ago (Aug. 26, 2025, 2:33 a.m.)
Issued	53 years, 10 months ago (Oct. 1, 1971)
Published	53 years, 10 months ago (Oct. 1, 1971)
Published Print	53 years, 10 months ago (Oct. 1, 1971)

Funders 0

None

BibTeX

@article{Schnaitman_1971, title={Solubilization of the Cytoplasmic Membrane of Escherichia coli by Triton X-100}, volume={108}, ISSN={1098-5530}, url={http://dx.doi.org/10.1128/jb.108.1.545-552.1971}, DOI={10.1128/jb.108.1.545-552.1971}, number={1}, journal={Journal of Bacteriology}, publisher={American Society for Microbiology}, author={Schnaitman, Carl A.}, year={1971}, month=oct, pages={545–552} }

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