Cytochemical model system for microsomal rat liver glucose-6-phosphate.

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Permeability of rat liver microsomal membrane to glucose 6-phosphate.

Light-scattering measurements of osmotically induced changes in the size of rat liver microsomal vesicles pre-equilibrated in a low-osmolality buffer revealed the following. (1) The increase in extravesicular osmolality by addition of glucose 6-phosphate or mannose 6-phosphate (25 mM each) caused a rapid shrinking of microsomal vesicles. After shrinkage, a rapid swelling phase (t1/2 approx. 22 ...

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Determination of liver microsomal glucose-6-phosphatase.

A procedure for the determination of liver microsomal glucose-6-phosphatase is described. Homogenization and ultracentrifrigation were used to prepare a precipitate whose character was defined by monitoring the desire enzyme activity which serves as a marker. Activity of the enzyme was determined by means of a sensitive colorimetric reaction for the product, inorganic phosphate. Non-enzymatic h...

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Liver Microsomal Glucose 6 - Phosphatase , Inorganic Pyrophosphatase , and Pyrophosphate - Glucose

Recently, we (1) described experiments which strongly supported the common identity of glucose 6-phosphatase,’ inorganic pyrophosphatase, pyrophosphate-glucose phosphotransferase, and mannose B-phosphate-glucose phosphotransferase activities present in a preparation obtained by ammonium sulfate fractionation of deoxycholate-dispersed rat liver microsomes. Previously, Segal, Washko, and Lee (2, ...

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Glucose-6-phosphate dehydrogenase in rat lung alveolar epithelial cells. An ultrastructural enzyme-cytochemical study.

Glucose-6-phosphate dehydrogenase (G6PD) is the key enzyme of the pentose phosphate pathway in carbohydrate metabolism, and it plays an important role in cell proliferation and antioxidant regulation within cells in various organs. Although marked cell proliferation and oxidant/antioxidant metabolism occur in lung alveolar epithelial cells, definite data has been lacking as to whether cytochemi...

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The multifunctional nature of classical microsomal glucose-6-phosphatase (D-glucose-6-P phosphohydrolase, EC 3.1.3.9) is now well documented (see, for example, refs. 1-8). Inherent in the reaction mechanism proposed by Arion and Nordlie2 to describe the variety of phosphohydrolase and phosphotransferase reactions catalyzed by the enzyme is the mutual competitive inhibition of various phosphohyd...

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ژورنال

عنوان ژورنال: Journal of Histochemistry & Cytochemistry

سال: 1976

ISSN: 0022-1554,1551-5044

DOI: 10.1177/24.5.180174