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Commentary
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denaturing of the enzyme in 6 M guanidinium chloride for 24 h and refolding by rapid dilution (1:20 v:v) into one of three solutions: benign buffer consisting of 50 mM KCl, 60 mM potassium phosphate pH 7.4, arginine buffer containing 0.67 M L-arginine-HCl, 60 mM potassium phosphate, pH 7.4, or arginine buffer containing 0.67 M L-arginine-HCl, 60 mM potassium phosphate, 50 mM Tris-HCl, pH 8.0, kinetics of refolding, overview. Enzyme refolding in arginine buffer, pH 7.4, is temperature-dependent, the rate of refolding follows apparent first-order kinetics. Omission of phosphate from the buffer does not affect the rate. The refolded enzyme form is much less thermostable than the native form
refolded from its isolated subunit after denaturation. Refolding of enzyme denatured in 6 M guanidine hydrochloride or of alpha- and beta-subunits isolated in the solvent requires the presence of either ethylene glycol or glycerol, optimally at 20-25% (v/v). MgGTP2- does not stimulate reactivation of the enzyme. Yields of 60% and 40% are obtained in the refolding of denatured enzyme and isolated subunits respectively
Results 1 - 2 of 2