6.3.5.2 | at low concentrations of the denaturants, up to 4.0 M urea and 1.2 M guanidine hydrochloride, inactivation is reversible. In 3.0-6.0 M guanidine hydrochloride the enzyme is extensively unfolded and partially, 15%, reassociable to the active form by removal of the denaturant. In 4.0 to 8.0 M urea and 1.2 to 3.0 M guanidine hydrochloride, the inactivation is irreversible due to the aggregation of the partially unfolded polypeptide chains |
1366 |