Letter | Published:

Reduction and Reoxidation of the Disulphide Bonds of Pepsinogen

Naturevolume 199pages11861187 (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.

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    Anfinsen, C. B., and Haber, E., J. Biol. Chem., 236, 1361 (1961).

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

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    Steiner, R. F., and Edelhoch, H., Chem Rev., 62, 457 (1962).

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

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  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.



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