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
An improved micromethod for the determination of glucose-6-phosphatase activity
β Scribed by T.R. Ricketts
- Book ID
- 115816738
- Publisher
- Elsevier Science
- Year
- 1963
- Tongue
- English
- Weight
- 241 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0009-8981
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π SIMILAR VOLUMES
Of the plethora of published methods for the determination of n-glucose, those which have the advantage of being both highly specific and sensitive have employed glucose oxidase (1) or hexokinase (2) as assay reagents.2 Although these methods have proved highly useful in many applications, they are
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