RNase, scrambled

The functional data demonstrate that the archaeal protein is an oxidant and reductant in fact, P/PDO is able to catalyze the oxidation of dithiol as well as the reduction of disulfides. The studies of the disulfide bond rearrangement were not successful at the low temperature used (30°) testing as substrate scrambled RNAse. 

Haber and Anfinsen (1962) have shown that reoxidation of RNase in 8 M urea or 4 M GuHCl gives a product which contains a great number of species with incorrectly formed S—S bonds. This scrambled ribonuclease is able to regain its native structure by exposure of the material to a small amount of reducing reagent and removal of urea to allow disulfide interchange (Fig. 5.12). 

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