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- W2024408540 abstract "1 Protease and diazobenzene sulfonate have been used to probe the transverse topology of the microsomal glucose-6-phosphatase system. 2 Treatment of intact microsomes with these reagents under the conditions used here did not affect the permeability of the membrane to mannose 6-phosphate, nucleoside diphosphatase, or dextran of 70 000 molecular weight. Nor did these treatments inactivate the hydrolytic site of glucose-6-phosphatase, a finding in agreement with earlier conclusions that this site is on the inside of the membrane. 3 On the other hand, treatment of intact microsomes with diazobenzene sulfonate or proteases does inactivate (or increase the apparent Km of) some other component which is rate-limiting for glucose-6-phosphatase activity in intact but not in disrupted microsomes. The simplest explanation for this phenomenon is that there is a protein carrier in the microsomal membrane which transports glucose 6-phosphate from the medium to the lumen, where it is hydrolyzed, and that diazobenzene sulfonate and proteases attack this carrier. 4 The lack of effect of these reagents on microsomal inorganic pyrophosphatase activity suggests that the glucose-6-phosphate carrier cannot transport pyrophosphate. 5 Finally, it was found that treatment of microsomes with ammonia breaks down their permeability barrier but also removes significant amounts of microsomal phospholipid and inactivates a number of microsomal enzymes. We do not recommend it as a general approach to altering microsomal permeability." @default.
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- W2024408540 date "1978-01-01" @default.
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- W2024408540 title "Evidence for the Involvement of a Glucose-6-Phosphate Carrier in Microsomal Glucose-6-Phosphatase Activity" @default.
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- W2024408540 doi "https://doi.org/10.1111/j.1432-1033.1978.tb12059.x" @default.
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