    1.1.3.13 | enzyme dissociation by 2 M KBr in 0.25 M potassium phosphate, pH 7.5, 0.3 mM EDTA, 5 mM 2-mercaptoethanol and 20% glycerol, for 4 days at 4°C. The inactive dissociated enzyme protein is renaturated, but still catalytically inactive, by assembly after removal of 2-mercaptoethanol and incubation with cofactor FAD. The enzyme activity is regained by incubation with the substrate. The dissociation process traverses through two FAD-associated intermediate proteins, one of whhich shows the enzyme activity. The catalytic reactivation is a slow process. Dynamic light scattering analysis, overview. DMSO and ethylene glycol are ineffective in dissociating this alcohol oxidase |
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