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Urea or guanidine hydrochloride(cas 50-01-1) denatured creatine kinase refolding and resurrection

In the past, we have studied the refolding and resurrection of creatine kinase, which is modified by urea or guanidine hydrochloride(cas 50-01-1), and found that under normal conditions, the denatured creatine kinase can be folded back to near natural conformation and the enzyme activity can be restored to near Enzyme activity. Compared with the dynamic process of refolding and resurrection, it was found that the refolding and resurrection of the enzyme molecules were not synchronized, and there was still a long slow process of resuscitation after the completion of the refolding.

We used OPTA specificity of the active site of the labeled enzyme to form a fluorescent group as a probe to detect the conformational changes in the active site during inactivation in a low concentration of urea solution. In this paper, we used this fluorescent probe to detect the In the process of refolding of creatine kinase, the conformational process of the active site of the enzyme was compared with the refolding of the whole molecule and the resurrection process of the enzyme.



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