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Denaturation under the action of guanidine hydrochloride(50-01-1)

Under the action of urea or guanidine, the inactivation rate of creatine kinase is much faster than that of the total conformational change of the enzyme molecule.
This paper reports that the method of studying substrate reaction in the presence of denaturing agent is smaller than that of single subunit, and five disulfide bonds to make the molecular structure more stable chymotrypsin, denaturation under the action of guanidine hydrochloride(50-01-1), inactivation and the corresponding renaturation, resurrection of the dynamic comparison.
The results show that inactivation is still faster than the conformational changes speed, resurrection is slower than the conformation of the recovery rate. The experimental results also show that the enzyme has been fully resurrected and non-denatured enzyme in the solution of the existence of some differences.



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