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- W2019918559 abstract "Abstract 1. 1. The effects of detergent and poly( l -lysine) (mol. wt 91,200) on phosphohydrolase activity of cat hepatic d -Glc-6-P phosphohydrolase (EC 3.1.3.9) have been investigated with the substrates: glucose 6-phosphate, mannose-6-phosphate and glucosamine-6-phosphate, at two temperatures 46 and 23°C. 2. 2. Optimal concentration of non-ionic detergent Triton X-100 was respectively 0.01% (v/v) at 46 C and 0.02% at 23°C. In all cases detergent produced an activation, especially important with mannose-6-phosphate and glucosamine-6-phosphate. 3. 3. Kinetic analysis revealed that Triton X-100 had no effect on the apparent Michaelis constant for glucose-6-phosphate, glucosamine-6-phosphate and for the lower K m for mannose-6-phosphate. 4. 4. Activation by polycations was related to their fixation on microsomal membrane and increased with the number of cationic groups per molecule. 5. 5. Poly( l -lysine) increased slightly the V values for the three substrates, but unlike detergent effect. quite pronounced lowering of K m values for mannose-6-phosphate and glucosamine-6-phosphate was observed. 6. 6. Results suggest that phosphohydrolase located on the luminal surface of the membrane was specific for hexose-6-phosphate." @default.
- W2019918559 created "2016-06-24" @default.
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- W2019918559 date "1981-01-01" @default.
- W2019918559 modified "2023-10-14" @default.
- W2019918559 title "comparison between the effect of polycations and detergent on the specificity of cat liver microsomal Glucose-6-Phosphatase" @default.
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- W2019918559 doi "https://doi.org/10.1016/0020-711x(81)90074-4" @default.
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