A new spectrophotometric arginase assay

Raymond L. Ward, P. Srere

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

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 colorimetric 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 2100 Å 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.

Original languageEnglish
Pages (from-to)102-106
Number of pages5
JournalAnalytical Biochemistry
Volume18
Issue number1
Publication statusPublished - Jan 1967

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Arginine
Assays
Ornithine
Urea
Arginase
Urease
Enzymes
Wavelength

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry

Cite this

A new spectrophotometric arginase assay. / Ward, Raymond L.; Srere, P.

In: Analytical Biochemistry, Vol. 18, No. 1, 01.1967, p. 102-106.

Research output: Contribution to journalArticle

Ward, RL & Srere, P 1967, 'A new spectrophotometric arginase assay', Analytical Biochemistry, vol. 18, no. 1, pp. 102-106.
Ward, Raymond L. ; Srere, P. / A new spectrophotometric arginase assay. In: Analytical Biochemistry. 1967 ; Vol. 18, No. 1. pp. 102-106.
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