Fig. 6.
Fig. 6. Thermal inactivation of wild-type and mutant R510Q RPK. / Thermal stability of wild-type (circles) and R510Q mutant (squares) RPK. Protein samples (100 μg/mL) were incubated at 53°C in a 50 mM potassium phosphate buffer pH 6.5, 100 mM KCl, and 1 mM EDTA. Aliquots were drawn at intervals for measuring residual activity, which was expressed as percentage of initial activity. Filled symbols were data obtained in the absence of FBP, and open symbols were data obtained in the presence of 1 mM FBP.

Thermal inactivation of wild-type and mutant R510Q RPK.

Thermal stability of wild-type (circles) and R510Q mutant (squares) RPK. Protein samples (100 μg/mL) were incubated at 53°C in a 50 mM potassium phosphate buffer pH 6.5, 100 mM KCl, and 1 mM EDTA. Aliquots were drawn at intervals for measuring residual activity, which was expressed as percentage of initial activity. Filled symbols were data obtained in the absence of FBP, and open symbols were data obtained in the presence of 1 mM FBP.

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