Advertisement

Detection of Disulfide-Linked Peptides by HPLC

  • Alastair Aitken
  • Michèle Learmonth
Protocol
  • 104 Downloads
Part of the Springer Protocols Handbooks book series (SPH)

Abstract

Classical techniques for determining disulfide bond patterns usually require the fragmentation of proteins into peptides under low pH conditions to prevent disulfide exchange. Pepsin or cyanogen bromide are particularly useful (see  Chapters 76 and  71 respectively).

Keywords

Cyanogen Bromide Iodoacetic Acid Peptide Bond Cleavage Reverse Phase HPLC Column Reductive Alkylation 
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.

References

  1. 1.
    Friedman, M., Zahnley, J. C., and Wagner, J.R. (1980) Estimation of the disulfide content of trypsin inhibitors as S-b-(2-pyridylethyl)-L-cysteine. Analyt. Biochem. 106, 27–34.PubMedCrossRefGoogle Scholar
  2. 2.
    Amons, R. (1987) xVapor-phase modification of sulfhydryl groups in proteins,. FEBS Lett. 212, 68–72.PubMedCrossRefGoogle Scholar
  3. 3.
    Toren, P., Smith, D., Chance, R., and Hoffman, J. (1988). Determination of Interchain Crosslinkages in Insulin B-Chain Dimers by Fast Atom Bombardment Mass Spectrometry. Analyt. Biochem. 169, 287–299.PubMedCrossRefGoogle Scholar

Copyright information

© Humana Press Inc., Totowa, NJ 2002

Authors and Affiliations

  • Alastair Aitken
    • 1
  • Michèle Learmonth
    • 2
  1. 1.Division of Biomedical and Clinical Laboratory Sciences, Membrane Biology GroupUniversity of EdinburghScotland, UK
  2. 2.Department of Biomedical SciencesUniversity of EdinburghScotland

Personalised recommendations