A spectrophotometric method for the determination of glucose-6-phosphatase activity
β Scribed by P. Gierow; B. Jergil
- Publisher
- Elsevier Science
- Year
- 1980
- Tongue
- English
- Weight
- 361 KB
- Volume
- 101
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
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. The formation of quinoneimine is followed directly on a spectrophotometer at 510 nm. The method described is as sensitive and accurate as conventional assays based on determination of phosphate released, and also works well in phosphate buffers.
π SIMILAR VOLUMES
A continuous spectrophotometric assay for glucose 6-phosphatase is described. The method uses glucose dehydrogenase and mutarotase as ancillary enzymes. Glucose 6-phosphatase activity is measured by following NADH formation at 340 nm. The method is linear, at least up to 38 mU in the test which corr
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 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
Elastiti ptqxtrationa stainetl wit11 Cotigo red ( 1,l or Oweitt (2) xc tliv substrates cOtntnottly uwl for the rlctvrtninatioti Of c~ladolytic activity.