PMID: 9428665Jan 15, 1998Paper

Three-state kinetic analysis of Chinese hamster dihydrofolate reductase unfolding by guanidine hydrochloride

Biochimica Et Biophysica Acta
J W WuJ M Zhou

Abstract

The unfolding behavior of dihydrofolate reductase from Chinese hamster in solutions of guanidine hydrochloride (GdnHCl) was studied. The GdnHCl-induced unfolding of the dihydrofolate reductase monitored by intrinsic fluorescence shows a biphasic transition, while the change in the enzyme activity is a single exponential process. The rate constant of inactivation is consistent with that of the fast conformational change. Therefore, the kinetic intermediate of protein unfolding should be a partially folded and inactive form. On the basis of the kinetic equation of substrate reaction in the presence of GdnHCl, all microscopic kinetic constants for the free enzyme and enzyme-substrate complexes have been determined. Both substrates, NADPH and 7,8-dihydrofolate, protect dihydrofolate reductase against inactivation.

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Citations

Jun 12, 2016·International Journal of Biological Macromolecules·Charu ThapliyalPratima Chaudhuri Chattopadhyay
Mar 18, 2008·Journal of Enzyme Inhibition and Medicinal Chemistry·Ferdinand C Chilaka, Charles O Nwamba

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