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1.4.1.3
complete loss of activity after incubation with 6 M guanidine hydrochloride or 7 M urea, no renaturation after dilution into 200 mM phosphate buffer
391613
1.4.1.3
monomeric and oligomeric enzyme show distinct behaviour on guanidine hydrochloride perturbation at neutral pH. The monomer denaturation, although complex, is reversible. Two fluorescent tryptophan classes are detectable in the monomer, monitoring the independent unfolding of two regions through a multistate transition. The oligomeric protein shows a complex denaturation pattern with the tendency to aggregate irreversibly at high denaturant concentration
718955
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