Letter | Published:

Reduction and Re-oxidation of the Disulphide Bonds of Soy Bean Trypsin Inhibitor

Nature volume 204, page 579 (07 November 1964) | Download Citation

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Abstract

SEVERAL examples have recently been reported of the partial or complete recovery of the native conformation and the biological activity of a protein following the reduction of all disulphide bridges under strongly denaturing conditions, such as 8 M urea or 5 M guanidine hydrochloride. The examples include insulin1, ribonuclease2, lysozyme3, and pepsinogen4. In each case the recovery was induced by removing the reducing agent and denaturing solvent and allowing the disulphide bridges to re-form spontaneously through re-oxidation of sulphydryl groups by atmospheric oxygen.

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References

  1. 1.

    , , , and , Scienta Sinica, 10, 84 (1961).

  2. 2.

    , , , and , Arch. Biochem. Biophys., Suppl. 1, 223 (1962).

  3. 3.

    , Fed. Proc., 21, 233 (1962).

  4. 4.

    , , , and , Nature, 199, 1186 (1963).

  5. 5.

    , Brookhaven Symp. Biol., No. 15, 184 (1962).

  6. 6.

    , and , J. Biol. Chem., 238, 931 (1963).

  7. 7.

    , and , Bioch., 1, 905 (1962).

  8. 8.

    , J. Amer. Chem. Soc., 76, 4331 (1954).

  9. 9.

    , and , Chem. Rev., 62, 457 (1962).

  10. 10.

    , Canad. J. Biochem. Physiol., 37, 1393 (1959).

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Author information

Affiliations

  1. Biological Macromolecules Branch, Physical Biochemistry Division, Naval Medical Research Institute, National Naval Medical Center, Bethesda, Maryland.

    • R. F. STEINER

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DOI

https://doi.org/10.1038/204579a0

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