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Guanidine hydrochloride(cas 50-01-1) is used in Chinese hamster dihydrofolate reductase

The main work of this paper is to apply the substrate reaction method to guanidine dihydrofolate reductase guanidine hydrochloride(cas 50-01-1), urea denaturation and p-chlorobenzoic acid modification activation kinetics. Although the kinetic theory of irreversible inhibition of enzyme activity has been applied to the study of enzyme activity in the absence of denaturant, previous studies have neglected an important problem associated with the determination of inactivation rate constants. 

In most protein denaturation experiments, high concentrations of denaturants may have a significant effect on the kinetic behavior of the enzyme reaction system, so the kinetic parameters measured in the absence of a denaturant are no longer applicable. 

We also deduced the kinetic equation of the substrate in the presence of the denaturant and reanalyzed the effect of the high concentration of guanidine hydrochloride on the Michaelisemesis of the enzyme catalyzed reaction. The inactivation kinetics of papain in the presence of guanidine hydrochloride(cas 50-01-1) showed that the substrate had no protective effect on the inactivation of papain.

 

 

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