๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Steady-state kinetic studies of arginase with an improved direct spectrophotometric assay

โœ 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.

โœฆ 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.


๐Ÿ“œ SIMILAR VOLUMES


A steady-state kineties study of myrosin
โœ S. Palmieri; O. Leoni; R. Iori ๐Ÿ“‚ Article ๐Ÿ“… 1982 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 317 KB

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