Radiometric method of determination of glucose-6-phosphatase activity
β Scribed by G. I. Meerov; Yu. P. Ryzhkova
- Publisher
- Springer US
- Year
- 1968
- Tongue
- English
- Weight
- 230 KB
- Volume
- 66
- Category
- Article
- ISSN
- 0007-4888
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π SIMILAR VOLUMES
A sensitive and rapid spectrophotometric method for determination of glucose-6-phosphatase activity is described. Glucose formed by the enzyme is oxidized by glucose oxidase to gluconolactone and hydrogen peroxide. The latter, phenol, and 4-aminoantipyrine are converted by peroxidase to quinoneimine
We present a method to determine glucose 6-phosphate activity. This assay measures the rate of glucose released in the glucose-6-phosphatase reaction. The glucose is oxidized to beta-D-gluconolactone by glucose dehydrogenase in a coupled reaction that uses NAD(P)+. The determination is rapid, reprod
A method is described for measuring the activity of glucose-6-phosphatase (EC 3.1.3.9) in rat liver. [U-W]Glucose 6-phosphate, as substrate, is converted by the enzyme to [Ylglucose and inorganic phosphate. The addition of ZnSO, and Ba(OH), at the end of the reaction precipitates phosphate and the u
We describe an automated, homogeneous, glucose oxidase-coupled method for the determination of glucose-6-phosphatase activity in tissue extracts. The method is based on measurement of the rate of glucose formation by the Trinder reaction, in which the end product is a quinoneimine dye which absorbs