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Detection of Non-Protein Components

  • Robert A. Copeland

Abstract

Within their natural biological environments, proteins often interact with other biological macromolecules, such as sugars, lipids, and nucleic acids. Sometimes these interactions are covalent, as in post-translational modifications of proteins, but more often involve non-covalent complex formation between the species. It is possible then, that non-protein com-ponents may occur in a protein sample, either as part of the biologically relevant active complex, or as contaminants that are not removed during purification. In this chapter we shall discuss methods for assessing the presence of the three most commonly occurring non-protein components in protein samples: nucleic acids, lipids from cell membranes, and covalently attached sugars in glycoproteins.

Keywords

Protein Glycosylation Ethidium Bromide Solution Lectin Blotting Tomato Lectin Deglycosylating Enzyme 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Casey, J. R.; Pirraglia, C. A.; and Reithmeier, R. A. F. (1992) J. Biol. Chem., 267, 11940–11948.PubMedGoogle Scholar
  2. Downs, T. R. and Wilfinger, W. W. (1983) Analyt. Biochem., 131, 538–547.PubMedCrossRefGoogle Scholar
  3. Gerard, C. (1990) Meth. Enzymol., 182, 529–539.PubMedCrossRefGoogle Scholar
  4. Harris, D. A., and Bashford, C. L. (1987) Spectrophotometry and Spectrofluorimetry: A Practical Approach, IRL Press, Oxford.Google Scholar
  5. Hughes, R. C. (1983) Glycoproteins, Chapman and Hall, New York.CrossRefGoogle Scholar
  6. Hugli, T. E. (1989) Techniques in Protein Chemistry, Academic Press, San Diego.Google Scholar
  7. Leach, B. S.; Colawn, J. F., Jr.; and Fish, W. W. (1980) Biochemistry,19, 57345741.Google Scholar
  8. Legros, M., and Kepes, A. (1985) Analyt. Biochem., 147, 497–502.PubMedCrossRefGoogle Scholar
  9. McGuckin, W. F., and McKenzie, B. F. (1958) Clin. Chem., 4, 476.PubMedGoogle Scholar
  10. Olmsted, J. B. (1981) J. Biol. Chem., 256, 11955–11957.PubMedGoogle Scholar
  11. Racusen, D. (1979) Analyt. Biochem., 99, 474–476.PubMedCrossRefGoogle Scholar
  12. Radin, N. S. (1969) Meth. Enzymol., 14, 245–254.CrossRefGoogle Scholar
  13. Skipski, V. P., and Barclay, M. (1969) Meth. Enzymol., 14, 530–598.CrossRefGoogle Scholar
  14. Wold, F. (1981) Ann. Rev. Biochem., 50, 783–814.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media Dordrecht 1994

Authors and Affiliations

  • Robert A. Copeland
    • 1
  1. 1.Experimental StationThe DuPont Merck Pharmaceutical CompanyWilmingtonUSA

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