AN INTERMEDIATE IN PH-INDUCED DISSOCIATION OF GLUTAMATE DEHYDROGENASE

We have carried out light-scatter and spectrophotometric stopped-flow studies on the acid induced dissociation of bovine liver L-glutamate dehydrogenase. The light-scatter intensity and the absorbance due to chromophore exposure follow the same time dependence, both changing only after a time lag of about 40 msec. The kinetics are consistent with a simple consecutive, two-step, irreversible reaction in which the first step converts β subunits into other forms identical in molecular weight and degree of folding and is followed by a second step in which these altered forms are converted into random coil, fully dissociated peptide chains. © 1969.