Spectrophotometric method for the determination of pancreatopeptidase E activity
✍ Scribed by W. Ardelt; S. Ksiȩżny; Izabella Niedźwiecka-Namysłowska
- Publisher
- Elsevier Science
- Year
- 1970
- Tongue
- English
- Weight
- 375 KB
- Volume
- 34
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
✦ Synopsis
Elastiti ptqxtrationa stainetl wit11 Cotigo red ( 1,l or Oweitt (2) xc tliv substrates cOtntnottly uwl for the rlctvrtninatioti Of c~ladolytic activity.
📜 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
A sensitive, rapid, quantitative method for the determination of the activities of the bifunctional frog epidermis enzyme, tyrosinase (E.C. 1.14.18. l), has been developed. It is a spectrophotometric method using p-coumaric acid and caffeic acid as substrates at pH 7.0. Lineweaver-Burk plots yielded
A new catalytic kinetic spectrophotometric method for the determination of oxalic acid has been described, based on its catalytic effect on the redox reaction between dichromate and rhodamine B, measured at the maximum absorption wavelength of 555 nm in sulphuric acid. Under the optimum conditions o
Superoxide dismutase (EC 1.15.1.1) has been assayed by a spectrophotometric method based on the inhibition of a superoxide-driven NADH oxidation. The assay consists of a purely chemical reaction sequence which involves EDTA, Mn(II), mercaptoethanol, and molecular oxygen, requiring neither auxiliary