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Quantitation of Cysteine Residues and Disulfide Bonds by Electrophoresis

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

Abstract

Amino acid analysis quantifies the molar ratios of amino acids per mole of protein. This generally gives a nonintegral result, yet clearly there are integral numbers of the amino acids in each protein. A method was developed by Creighton (1) to count integral numbers of amino acid residues, and it is particularly useful for the determination of cysteine residues. Sulfhydryl and disulfide groups are of great structural, functional, and biological importance in protein molecules. For example, the Cys sulfhydryl is essential for the catalytic activity of some enzymes (e.g., thiol proteases) and the interconversion of Cys SH to Cystine S—S is directly involved in the activity of protein disulfide isomerase (2). The conformation of many proteins is stabilized by the presence of disulfide bonds (3), and the formation of disulfide bonds is an important posttranslational modification of secretory proteins (4).

Keywords

Disulfide Bond Protein Disulfide Isomerase Ammonium Persulfate Fume Hood Succinic Anhydride 
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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Copyright information

© Humana Press Inc., Totowa, NJ 1996

Authors and Affiliations

  • Alastair Aitken
    • 1
  • Michèle Learmonth
    • 1
  1. 1.National Institute for Medical ResearchMill Hill, LondonUK

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