Modifications of Hydrolytic and Synthetic Activities of Liver Microsomal Glucose 6-Phosphatase
نویسندگان
چکیده
منابع مشابه
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...
متن کاملLiver 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, ...
متن کاملIdentification and purification of a liver microsomal glucose 6-phosphatase.
1. Hepatic glucose 6-phosphatase activity was purified 65-fold in good yield over that in cholate-solubilized microsomal fractions. 2. This preparation still contained five major polypeptides and numerous minor contaminants. 3. The smallest of the five major polypeptides (Mr approx. 18 500) could be purified from heat-treated microsomal fractions. 4. Antisera raised against the heat-stable prot...
متن کاملInhibition by nucleotides of liver microsomal glucose-6-phosphatase.
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...
متن کاملThermal stability of microsomal glucose-6-phosphatase.
The thermal stability of glucose-6-phosphatase in rat liver microsomes was examined in untreated and cholate-treated microsomes. Activity of the enzyme was measured with both glucose-6-P and mannose-6-P as substrates. Heat treatment did not cause glucose-6-phosphatase activity to decline to zero with a single rate constant in untreated microsomes. Instead, heat treatment produced an enzyme with...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1972
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)45461-6