Skip to main content

Chemical Cleavage of Proteins

  • Protocol
Basic Protein and Peptide Protocols

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 32))

Abstract

There is a variety of chemical reactions known to result in the cleavage of the peptide bond. Some are nonspecific—for instance, 6M hydrochloric acid at 110°C for 24 h hydrolyzes a polypeptide to a mixture of single amino acids. Others show some discrimination, however, as to the precise nature of the amino acid residues around the bond to be broken. Some of these methods are sufficiently specific to be of use, for instance, for generating peptides for primary structure determination. These methods usefully augment those that use proteolytic enzymes (see Chapter 32), especially since they tend to act at positions occupied by less common amino acids and so generate large peptides.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Protocol
USD 49.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 129.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 169.00
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 169.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  1. Fontana, A. and Gross, E. (1986) Fragmentation of polypeptides by chemical methods, in Practical Protein Chemistry—A Handbook (Dabre, A., ed.), Wiley, Chichester, pp. 67–120.

    Google Scholar 

  2. Horn, M. and Laursen, R. A. (1973) Solid-phase Edman degradation. Attachment of carboxyl-terminal homoserine peptides to an insoluble resin. FEBS Lett. 36, 285–288.

    Article  PubMed  CAS  Google Scholar 

  3. Huang, H. V., Bond, M. W., Hunkapillar, M. W., and Hood, L. E. (1983) Cleavage at tryptophanyl residues with dimethyl sulfoxide-hydrochloric acid and cyanogen bromide. Meth. Enzymol. 91, 318–324.

    Article  PubMed  CAS  Google Scholar 

  4. Ingris, A. S. (1983) Cleavage at aspartic acid. Meth. Enzymol. 91, 324–332.

    Article  Google Scholar 

  5. Wachter, E. and Werhahn, R. (1980) Cleavage of Trp-, Tyr-, and His-bonds suited for attachment to amino-supports and subsequent Edman degradation, in Methods in Peptide and Protein Sequence Analysis (Birr, C., ed.), Elsevier/North Holland, Amsterdam, pp. 21–33.

    Google Scholar 

  6. Landon, M. (1977) Cleavage at aspartyl-prolyl bonds. Methods Enzymol. 47, 145–149.

    Article  PubMed  CAS  Google Scholar 

  7. Bornstein, P. and Balian, G. (1977) Cleavage at cysteine at Asn-Gly bonds with hydroxylamine. Methods Enzymol. 47, 132–145.

    Article  PubMed  CAS  Google Scholar 

  8. Stark, G. R. (1977) Cleavage at cysteine after cyanylation. Methods Enzmol. 47,129–132.

    Article  CAS  Google Scholar 

  9. Otieno, S. (1978) Generation of a free α-amino group by Raney Nickel after 2-nitro-thiocyanobenzoic acid cleavage at cysteine residues: Application to automated sequencing. Biochemistry 17, 5468–5474.

    Article  PubMed  CAS  Google Scholar 

  10. Ramachandran, L. K. and Witkop, B. (1976) N-Bromosuccinimide cleavage of peptides. Method Enymol. 11, 283–299.

    Article  Google Scholar 

  11. Iwai, K. and Ando, T. (1976) N→O acyl rearrangement. Methods Enzymol. 11, 236–282.

    Google Scholar 

  12. Cohen, L. A. and Farber, L. (1967) Cleavage of tyrosyl-peptide bonds by electrolytic oxidation. Methods Enzymol. 11, 299–308.

    Article  CAS  Google Scholar 

  13. Fontana, A. (1972) Modification of tryptophan with BNPS skatole (2-(2-nitro-phenylsulfenyl)-3-methyl-3-bromoindolenine). Methods Enzymol. 25, 419–423.

    Article  CAS  Google Scholar 

  14. Ozols, J. and Gerard, C. (1977) Covalent structure of the membranous segment of horse cytochrome b5. Chemical cleavage of the native hemprotein. J. Biol. Chem. 252, 8549–8553.

    PubMed  CAS  Google Scholar 

  15. Savige, W. E. and Fontana, A. (1977) Cleavage of the tryptophanyl peptide bond by dimethyl sulfoxid-hydrobromic acid. Methods Enzymol. 47, 469–468.

    Article  Google Scholar 

  16. Fontana, A., Dalzoppo, D., Grandi, C., and Zambonin, M. (1983) Cleavage at tryptophan with o-iodosobenzoic acid. Methods Enzymol. 91, 311–318.

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1994 Humana Press Inc., Totowa, NJ

About this protocol

Cite this protocol

Smith, B.J. (1994). Chemical Cleavage of Proteins. In: Walker, J.M. (eds) Basic Protein and Peptide Protocols. Methods in Molecular Biology™, vol 32. Humana Press. https://doi.org/10.1385/0-89603-268-X:297

Download citation

  • DOI: https://doi.org/10.1385/0-89603-268-X:297

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-268-2

  • Online ISBN: 978-1-59259-519-8

  • eBook Packages: Springer Protocols

Publish with us

Policies and ethics