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- W2054394204 abstract "1. Evidence presented supports the hypothesis that the endoplasmic reticular membrane enzyme, glucose-6-phosphatase, with its related activities, inorganic pyrophosphatase and inorganic pyrophosphate-glucose phosphotransferase, exists within the membrane in two different forms or different degrees of accessibility to substrate. In membrane areas having attached ribosomes the enzyme is predominately in an “activated” configuration while that in the smooth membranes is in a less active or potential form. 2. The three enzyme activities studied have higher pH optima and, under normal assay conditions, greater specific activities in the ribosome-rich, “rough” subfractions of liver microsomes than in “smooth” subfractions of the same preparations. 3. On activation by pretreatment with NH4OH or deoxycholate, the enzymatic activities and pH optima of the smooth subfractions are shifted to higher values to a greater extent than are those of the rough. 4. When comparisons are made on optimally activated samples, total, rough and smooth membranes exhibit approximately the same enzymatic activities and identical elevated pH optima. 5. Despite great quantitative differences in the enzymatic activities of preparations from livers of fed, fasted, phenobarbital-treated and alloxan-diabetic rats, the same patterns of differences between enzyme activities of rough and smooth membranes was observed for all animals. 6. Phenobarbital-treated animals, in which there is a large proliferation of smooth membranes, have been found by others to exhibit a lower specific activity of liver glucose-6-phosphatase than do control animals. This may be explained in part by the preponderance of less active enzyme in the smooth membranes." @default.
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- W2054394204 date "1971-03-01" @default.
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- W2054394204 title "Different properties of glucose-6-phosphatase and related enzymes in rough and smooth endoplasmic reticular membranes" @default.
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- W2054394204 doi "https://doi.org/10.1016/0005-2736(71)90369-5" @default.
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