Abstract
Summary
The utilization of glucose and other nonphosphorylated sugars by partially purified normal G-6-PD and G-6-PD Mediterranean was investigated. Both enzymes have the capacity to oxidize glucose with a Km of approximately 0.8 M. The utilization of glucose by both enzymes was markedly stimulated by the presence of bicarbonate, and the activity with Mediterranean enzyme was greater than that of normal G-6-PD. The pH optimum of utilization of glucose by the two enzymes was very similar. Galactose, 2-deoxyglucose, fructose, mannose, and ribose did not serve as substrate for either type of G-6-PD.
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