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Reduction and Reoxidation of the Disulphide Bonds of Pepsinogen

Abstract

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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References

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FRATTALI, V., STEINER, R., MILLAR, D. et al. Reduction and Reoxidation of the Disulphide Bonds of Pepsinogen. Nature 199, 1186–1187 (1963). https://doi.org/10.1038/1991186a0

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