Letter | Published:

Reduction and Reoxidation of the Disulphide Bonds of Pepsinogen

Nature volume 199, pages 11861187 (21 September 1963) | Download Citation



Anfinsen and Haber have shown that the disulphide bonds of ribonuclease (RNase) can be cleaved by treatment of the native protein in 8 M urea with mercaptoethanol1. On exposure to molecular oxygen, reduced RNase is re-oxidized with complete regeneration of secondary and tertiary structure. The kinetics of the reaction indicate either that pairing of the correct half-cystine residues is a random process with the molecule undergoing subsequent structural rearrangement to yield the native form2; or, alternatively, that the reduced protein may be sufficiently structurally similar to the native enzyme to allow correct matching and reoxidation of the half-cystinyl residues, even in the absence of the disulphide bridges3.

Access optionsAccess options

Rent or Buy article

Get time limited or full article access on ReadCube.


All prices are NET prices.


  1. 1.

    , and , J. Biol. Chem., 236, 1361 (1961).

  2. 2.

    , , , and , Proc. U.S. Nat. Acad. Sci., 47, 1309 (1961).

  3. 3.

    , and , J. Biol. Chem., 237, 1839 (1962).

  4. 4.

    , and , J. Biol. Chem., 238, 653 (1963).

  5. 5.

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

  6. 6.

    , in Crystalline Enzymes, edit. by Northrop, J. H., Kunitz, M., and Herriott, R. M., second ed., 305 (Columbia Univ. Press, New York, 1948).

  7. 7.

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

  8. 8.

    , J. Biol. Chem. (in the press).

  9. 9.

    , J. Gen. Physiol., 41, 441 (1958).

Download references

Author information


  1. Department of Biochemistry, Georgetown University, Washington 7, D.C.

  2. Physical Biochemistry Division, Naval Medical Research Institute, Bethesda 14, Md.

    • R. F. STEINER
    •  & D. B. S. MILLAR
  3. National Institute of Arthritis and Metabolic Diseases, National Institutes of Health, Bethesda 14, Md.



  1. Search for V. FRATTALI in:

  2. Search for R. F. STEINER in:

  3. Search for D. B. S. MILLAR in:

  4. Search for H. EDELHOCH in:

About this article

Publication history




Further reading


By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.