Abstract
Glucose-6-phosphatase (E.C.3.1.3.9) is a multicomponent system consisting of the glucose-6-phosphate enzyme with its active site located on the luminal side of the endoplasmic reticulum (ER) and three translocases which allow entry of glucose-6-phosphate (T, ) and entry of pyrophosphate and exit of phophate (T2) and exit of glucose (T,) from the lumen of the ER (Arion et al., 1980). The routinely used method of assaying the translocase activities is indirect and involves complex calculation of the rate limitations imposed on the glucose-6-phosphatase system by the translocases (Arion et al., 1980). The combination of rapid transport rates and small internal volumes poses a considerable experimental problem in direct assays of transport (Nicholls, 1982). A complex direct assay using centrifugation through
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