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A new spectrophotometric arginase assay

โœ Scribed by Raymond L. Ward; Paul A. Srere

Publisher
Elsevier Science
Year
1967
Tongue
English
Weight
183 KB
Volume
18
Category
Article
ISSN
0003-2697

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โœฆ Synopsis

We wish to report a new method for the assay of arginase (L-arginine amidinohydrolase, EC 3.5.3.1). Arginase, the terminal enzyme of the urea-ornithine cycle (1)) catalyzes the cleavage of arginine to ornithine and urea. Present assays for arginase determine the released urea either by a calorimetric procedure (2) or by a manometric procedure with urease (3). Our new assay 'is a spectrophotometric method based on the fact that the absorbancy of arginase below 21OOA is larger than the combined absorbancies of ornithine and urea. A cleavage of arginine catalyzed by the enzyme thus results in a net decrease in absorbancy at these wavelengths, allowing a rapid and accurate assay for arginase activity.

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