Abstract
The permeability of rat liver microsomes to glucose was investigated in relation to the hexose-6-phosphate dehydrogenase system (EC 1.1.1.47). It was found that glucose-6-phosphate dehydrogenase activity could be assayed with NADP as coenzyme in both untreated and detergent-treated microsomes. However, when glucose was used as substrate, activity was only measurable in detergent-treated microsomes. Moreover, radioactive glucose added to microsomes in a variety of experimental conditions was never taken up by the vesicles. Our results indicate that NADP (or NAD) availability is probably not the reason for the absence of glucose dehydrogenase activity in untreated microsomes but rather membrane impermeability to glucose would account for the complete latency observed. This finding calls for a reevaluation of glucose transport in relation to other enzymes of the endoplasmic reticulum, such as glucose-6-phosphatase.
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