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The Protein Protocols Handbook pp 581–583Cite as

Detection of Disulfide-Linked Peptides by HPLC

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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).

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References

  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.

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  2. Amons, R. (1987) xVapor-phase modification of sulfhydryl groups in proteins,. FEBS Lett. 212, 68–72.

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  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.

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Author information

Authors and Affiliations

  1. Division of Biomedical and Clinical Laboratory Sciences, Membrane Biology Group, University of Edinburgh, Scotland, UK

    Alastair Aitken

  2. Department of Biomedical Sciences, University of Edinburgh, Scotland

    Michèle Learmonth

Authors
  1. Alastair Aitken
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  2. Michèle Learmonth
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Editor information

Editors and Affiliations

  1. University of Hertfordshire, Hatfield, UK

    John M. Walker

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© 2002 Humana Press Inc., Totowa, NJ

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Cite this protocol

Aitken, A., Learmonth, M. (2002). Detection of Disulfide-Linked Peptides by HPLC. In: Walker, J.M. (eds) The Protein Protocols Handbook. Springer Protocols Handbooks. Humana Press. https://doi.org/10.1385/1-59259-169-8:581

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  • DOI: https://doi.org/10.1385/1-59259-169-8:581

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-940-7

  • Online ISBN: 978-1-59259-169-5

  • eBook Packages: Springer Book Archive

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