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생화학분자생물학회 (Korean Society for Biochemistry and Molecular Biology)
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Disrupting Escherichia coli: A Comparison of Methods

  • Benov, Ludmil (The Department of Biochemistry, Faculty of Medicine, Kuwait University) ;
  • Al-Ibraheem, Jameela (The Department of Biochemistry, Faculty of Medicine, Kuwait University)
  • 발행 : 2002.07.31
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초록

The often-encountered problem of disrupting bacteria for the purpose of extracting soluble protein has generated various methods. Many require specialized equipment. Very often, especially during preliminary studies, investigators need a simple, fast, and inexpensive method for cell disruption that preserves biological activity. This paper compares some simple and inexpensive methods for cell disruption, such as bead-vortexing, freesing-thawing, French pressing, and sonication. It also provides some tips to increase protein yield and preserve biological activity. If performed under optimal conditions, bead-vortexing gives protein yields that are comparable to French pressing and sonication. It also preserves the activities of labile enzymes and releases periplasmic enzymes. Vortexing with glass beads appears to be the simplest method for cell disruption.

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참고문헌

  1. Benov, L., Sage, H. and Fridovich, I. (1997) The copper- and zinc-containing superoxide dismutase from Escherichia coli: Molecular weight and stability. Arch. Biochem. Biophys. 340, 305-310. https://doi.org/10.1006/abbi.1997.9940
  2. Gardner, P. and Fridovich, I. (1991) Superoxide sensitivity of the Escherichia coli aconitase. J. Biol. Chem. 266, 19328-19333.
  3. Gardner, P. and Fridovich, I. (1992) Inactivation-reactivation of aconitase in Escherichia coli. A sensitive measure of superoxide radical. J. Biol. Chem. 266, 19328-19333.
  4. Hasan, N. and Nester, E. (1978) Dehydroquinate synthase in Bacillus subtilis. An enzyme associated with chorismate synthase and flavin reductase. J. Biol. Chem. 253, 4999-5004.
  5. Hayashi, S. and Lin, R. C. C. (1967) Purification and properties of glycerol kinase from Escherichia coli. J. Biol. Chem. 212, 1030-1035.
  6. Imlay, I. and Linn, S. (1987) Mutagenesis and stress response induced in Escherichia coli by hydrogen peroxide. J. Bacteriol. 169, 2967-2976. https://doi.org/10.1128/jb.169.7.2967-2976.1987
  7. Liochev, S. and Fridovich, I. (1993) Modulation of the fumarases of Escherichia coli in response to oxidative stress. Arch. Biochem. Biophys. 301, 379-384. https://doi.org/10.1006/abbi.1993.1159
  8. Lowry, O. H., Rosebrough, N. F., Farr, A. L. and Randall, R. J. (1951) Protein measurement with the Folin phenol reagent. J. Bioi. Chem. 193, 265-275.
  9. McCord, J. M. and Fridovich I. (1969) Superoxide dismutase: An enzymatic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244, 6049-6055
  10. Song, D. D. and Jacques, N. A. (1997) Cell disruption of Escherichia coli by glass bead stirring for the recovery of recombinant proteins. Anal. Biochem. 248, 300-301. https://doi.org/10.1006/abio.1997.2149
  11. Woods, S. A., Schwartzbach, S. D. and Guest, J. R. (1988) Two biochemically distinct classes of fumarase in Escherichia coli. Biochim. Biophys. Acta 954, 14-26. https://doi.org/10.1016/0167-4838(88)90050-7

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