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A membrane filter procedure developed by Igarashi et al. (1984) for the measurement of glucose 6-phosphate uptake by the microsomes has been demonstrated to be a good method for assaying glucose-6-phosphate translocase, an obligatory component of the microsomal glucose-6-phosphatase system. When glucose-6-phosphate translocase was assayed in developing and diabetic rat livers independently of hexose-6-phosphate phosphohydrolase, another obligatory component of the glucose-6-phosphatase system, the two activities were found to undergo alterations, whose profiles, however, were quite distinct from each other. The profile of the microsomal glucose-6-phosphatase activity resembles the profile of the phosphohydrolase activity rather than that of the translocase activity, suggesting that the phosphohydrolase may be rate-limiting at least under these conditions. AH-109A, a strain of transplantable rat ascites hepatoma, was found to lack both glucose-6-phosphate translocase and hexose-6-phosphate phosphohydrolase activities.
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