Glucose-6-phosphatase activity in rat bone.
نویسندگان
چکیده
منابع مشابه
Glucose-6-phosphatase activity in regenerating, embryonic, and newborn rat liver.
Studies on carbohydrate metabolism have dem onstrated important differences between normal liver and hepatoma (3, 9,17). Since it seemed that the deviation of the carbohydrate metabolism of the hepatoma from that of the normal liver starts at the utilization of the G-6-P1 ester, a systematic study of G-6-P utilization was undertaken in this laboratory. One of the most important pathways of G-6-...
متن کاملGlucose-6-phosphatase deficiency
Glucose-6-phosphatase deficiency (G6P deficiency), or glycogen storage disease type I (GSDI), is a group of inherited metabolic diseases, including types Ia and Ib, characterized by poor tolerance to fasting, growth retardation and hepatomegaly resulting from accumulation of glycogen and fat in the liver. Prevalence is unknown and annual incidence is around 1/100,000 births. GSDIa is the more f...
متن کاملSepsis-induced depression of rat glucose-6-phosphatase gene expression and activity.
Sepsis in rats decreases the hepatic expression of the gluconeogenic enzyme glucose-6-phosphatase (G6Pase). The aim of this study was to investigate the relationship among G6Pase transcription, mRNA, enzymatic activity, and serum glucose levels at different intervals during mild or fulminant sepsis. Both fulminant and mild sepsis immediately decreased hepatic G6Pase mRNA levels. In mild sepsis,...
متن کاملThe glucose-6-phosphatase system.
Glucose-6-phosphatase (G6Pase), an enzyme found mainly in the liver and the kidneys, plays the important role of providing glucose during starvation. Unlike most phosphatases acting on water-soluble compounds, it is a membrane-bound enzyme, being associated with the endoplasmic reticulum. In 1975, W. Arion and co-workers proposed a model according to which G6Pase was thought to be a rather unsp...
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: Agricultural and Biological Chemistry
سال: 1985
ISSN: 0002-1369,1881-1280
DOI: 10.1271/bbb1961.49.2455