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Protein Sequencing Protocols pp 271–284Cite as

Chemical Modification of Proteins for Sequence Analysis

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Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 64))

Abstract

The two most widely used applications for chemical modification are in primary structure analysis and in the identification of essential groups involved in the binding and catalytic sites of proteins. The methods discussed here are those used frequently in primary structure analysis. Chemical modifications involving protein “active center” identification are the subject of a review by Pfleiderer (1).

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References

  1. Pfleiderer, G. (1985) Chemical modification of proteins, in Modern Methods in Protein Chemistry, Review Articles, vol. 2 (Tschesche, H., ed.), Walter de Gruyter, Berlin, pp. 207–259.

    Google Scholar 

  2. Hewick, R. M., Hunkapillar, M. W., Hood, L. E., and Dreyer, W. J. (1981) A gas-liquid solid phase peptide and protein sequenator. J. Biol. Chem. 256, 7990–7997.

    CAS  Google Scholar 

  3. Applied Biosystems (1992) New multimode sequencer permits range of sequencing conditions. Applied Biosystems Reporter 17, 6–7.

    Google Scholar 

  4. Glazer, A. N., Delange, R. J., and Sigman, D. S. (1975) Chemical characterization of proteins and their derivatives, in Chemical Modification of Proteins (Work, T. S. and Work, E., eds.), North Holland, American Elsevier, Amsterdam, pp. 21–24.

    Google Scholar 

  5. Amons, R. (1987) Vapor phase modification of sulphdryl groups in proteins. Febs Lett. 122, 68–72.

    Article  Google Scholar 

  6. Applied Biosystems (1991) Efficient recovery of pyridylethylated CPP for high sensitivity protein sequencing. Application Note #2.

    Google Scholar 

  7. Sheer, D. (1990) Sample Centrifugation onto membranes for sequencing. Anal. Biochem. 187, 76–83.

    Article  CAS  Google Scholar 

  8. Fullmer, C. S. (1984) Identification of cysteine containing peptides in protein digests by high performance chromatography. Anal. Biochem. 142, 336–339.

    Article  CAS  Google Scholar 

  9. Brune, D. C. (1992) Alkylation of Cysteine with Acrylamide for Protein Sequence Analysis. Anal. Biochem. 207, 285–290.

    Article  CAS  Google Scholar 

  10. Applied Biosystems (1995) Derivatization of cysteine residues in solution for protein sequencing. User Bulletin Number 61.

    Google Scholar 

  11. Walker, J. E., Carne, A. F., Runswick, M. J., Bridgen, J., and Harris, J. I. (1980) D-Glyceraldehyde-3-phosphate dehydrogenase. Complete amino-acid sequence of the enzyme from Bacillus stearothermophilus. Eur. J. Biochem. 108, 549–565.

    Article  CAS  Google Scholar 

  12. Levy, M., Fishman, L., and Schenkein, I. (1970) Mouse submaxillary gland proteases, in Methods in Enzymology, vol. XIX, Proteolytic Enzymes (Perlman, G. E. and Lorand, L., eds.), Academic, New York, pp. 672–681.

    Chapter  Google Scholar 

  13. Mitchell, W. M. and Harrington, W. F. (1970) Clostripain, in Methods in Enzymology, vol XIX Proteolytic Enzymes (Perlman, G. E. and Lorand, L., eds.), Academic, New York, pp. 635–642.

    Chapter  Google Scholar 

  14. Thomas, K. A. and Bradshaw, R. A. (1981) γ-Subunit of mouse submaxillary gland 7S nerve growth factor: an endopeptidase of the serine family, in Methods in Enzymology, vol 80, Proteolytic Enzymes, part C (Lorand, L.,ed.), Academic, New York, pp. 609–620.

    Chapter  Google Scholar 

  15. Tous, G. I., Fausnaugh, J. L., Akinyosoye, O., Hackland, H., Winter-Cash, P., Vitorica, F. J., and Stein, S. (1989) Amino acid analysis on polyvinylidene difluoride membranes. Anal. Biochem. 179, 50–55.

    Article  CAS  Google Scholar 

  16. Applied Biosystems (1992) Premix buffer for protein sequencers. User Bulletin #43.

    Google Scholar 

  17. Jue, R. A. and Hale, J. E. (1994) On-line procedures for alkylation of cysteine residues with 3-bromopropylamine prior to protein sequence analysis. Anal. Biochem. 221, 374–378.

    Article  CAS  Google Scholar 

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Author information

Authors and Affiliations

  1. Institute of Cancer Research, London, UK

    Alex F. Carne

  2. Thermo Bioanalysis, Hemel Hempstead, UK

    Sally U

Authors
  1. Alex F. Carne
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  2. Sally U
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Editor information

Editors and Affiliations

  1. Celltech Therapeutics, Slough, UK

    Bryan John Smith

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© 1997 Humana Press Inc.

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Carne, A.F., U, S. (1997). Chemical Modification of Proteins for Sequence Analysis. In: Smith, B.J. (eds) Protein Sequencing Protocols. Methods in Molecular Biology™, vol 64. Humana Press, Totowa, NJ. https://doi.org/10.1385/0-89603-353-8:271

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  • DOI: https://doi.org/10.1385/0-89603-353-8:271

  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-0-89603-353-5

  • Online ISBN: 978-1-59259-550-1

  • eBook Packages: Springer Protocols

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