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- W1998873882 abstract "Carbamyl-P:glucose and PP 2 :glucose phosphotransferase, but not inorganic pyrophosphatase, activities of the hepatic microsomal glucose-6-phosphatase system demonstrate a time-dependent lag in product production with 1 mM phosphate substrate. Glucose-6-P phosphohydrolase shows a similar behavior with [glucose-6-P] ≦ 1.10 mM, but inorganic pyrophosphatase activity does not even at the 0.05 or 0.02 mM level. The hysteric behavior is abolished when the structural integrity of the microsomes is destroyed by detergent treatment. Calculations indicate that an intramicrosomal glucose-6-P concentration of between 20 and 40 μM must be achieved, whether in response to exogenously added glucose-6-P or via intramicrosomal synthesis by carbamyl-P: glucose or PP 1 : glucose phosphotransferase activity, before the maximally active form of the enzyme system is achieved. It is suggested that translocase T 1 , the transport component of the glucose-6-phosphatase system specific for glucose-6-P, is the target for activation by these critical intramicrosomal concentration of glucose-6-P." @default.
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- W1998873882 date "1991-12-01" @default.
- W1998873882 modified "2023-09-26" @default.
- W1998873882 title "Hysteretic behavior of the hepatic microsomal glucose-6-phosphatase system" @default.
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- W1998873882 doi "https://doi.org/10.1016/0167-4838(91)90445-6" @default.
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