Letter | Published:

Determination of Disulphide Groups in Proteins

Nature volume 212, pages 294295 (15 October 1966) | Download Citation

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Abstract

RELATIVELY simple methods are available for the determination of sulphydryl groups in proteins1. The determination of disulphide groups is, however, more difficult and the methods available are more laborious and less accurate. Most of the methods used for the determination of disulphide groups are based on the reduction of these groups followed by amperometric determination of liberated thiols2. Alternative to these procedures are those using exchange with dinitrophenylcystine3, oxidation with performic acid4, or reduction and alkylation with mono-iodacetate5. This communication deals with the method recently used in our laboratory for the determination of disulphide groups using sodium borohydride (NaBH4) in 8 molar urea as reducing agent6,7 and 5,5′-dithiobis (2-nitrobenzoic) acid (DTNB) as a thiol disulphide exchanger8.

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Affiliations

  1. Department of Biological Chemistry, University of Rome, Italy.

    • D. CAVALLINI
    • , M. T. GRAZIANI
    •  & S. DUPRÉ

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https://doi.org/10.1038/212294a0

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