Plant myrosinase (EC 3.2.3.1) catalyzes the hydrolysis of mustard oil glucosides to isothiocyanate, glucose, and sulfate. We have developed a spectrophotometric assay for myrosinase activity with sinigrin as substrate which measures the decomposition of the allylglucosinolate by the decrease in abso
โฆ LIBER โฆ
Steady-state kinetic studies of arginase with an improved direct spectrophotometric assay
โ Scribed by C.Nick Pace; Andres Buonanno; Jeannie Simmons-Hansen
- Publisher
- Elsevier Science
- Year
- 1980
- Tongue
- English
- Weight
- 361 KB
- Volume
- 109
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
โฆ Synopsis
A direct spectrophotometric assay for arginase developed by R. L. Ward and P. A. Srere t 1967. At~crl. Biochem. 18, 102) is extended so that it can be used at pH 7.5 or 9.5. at higher substrate concentrations, for assaying crude sources of arginase. and for steady-state kinetic studies of the enzyme. Steady-state kinetic studies of beef and rat liver arginase are reported and compared with Gmilar results obtained using other assay procedures. A number of problems encountered in steady-state kinetic studies of argina\e are discussed.
๐ SIMILAR VOLUMES
A steady-state kineties study of myrosin
โ
S. Palmieri; O. Leoni; R. Iori
๐
Article
๐
1982
๐
Elsevier Science
๐
English
โ 317 KB