Two techniques for determining enzyme kinetic constants using isothermal titration microcalorimetry are presented. The methods are based on the proportionality between the rate of a reaction and the thermal power (heat/time) generated. (i) An enzyme can be titrated with increasing amounts of substra
Enzyme electrode-based kinetic assays of enzyme activities
β Scribed by C.R. Gebauer; M.E. Meyerhoff; G.A. Rechnitz
- Publisher
- Elsevier Science
- Year
- 1979
- Tongue
- English
- Weight
- 303 KB
- Volume
- 95
- Category
- Article
- ISSN
- 0003-2697
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β¦ Synopsis
Potentiometric enzyme electrodes for urea, AMP, and adenosine have been used for the kinetic assays of arginase (EC 3.5.3.1), 3':5'-cyclic-nucleotide phosphodiesterase (EC 3.1.4.17), and 5'-nucleotidase (EC 3.1.3.5), respectively. The initial rate of potential change, after addition of the enzyme to the substrate solution, is directly proportional to the enzyme activity present. Arginase assays were found to be reproducible to a relative precision of 13% or better and applicable to the direct measurement of arginase activity in beef liver homogenates.
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