Clinical Chemistry
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Clinical Chemistry 35: 654-658, 1989;
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Clinical Chemistry, Vol 35, 654-658, Copyright © 1989 by American Association for Clinical Chemistry

Enzymic urea assay: a new colorimetric method based on hydrogen peroxide measurement

F Lespinas, G Dupuy, F Revol and C Aubry
Laboratoire d'Analyses Medicales, Montpon-Menesterol, France.

We describe a new enzymic colorimetric method in which urea is measured in serum by use of a single reagent mixture. Ammonia produced by urea hydrolysis, catalyzed by urease, reacts with glutamate and ATP in the presence of glutamine synthetase. The ADP so produced is assayed in reactions catalyzed sequentially by pyruvate kinase and pyruvate oxidase in a system that generates hydrogen peroxide. The hydrogen peroxide is measured at 500 or 550 nm in a reaction catalyzed by horseradish peroxidase, with phenol/4-aminophenazone as the chromogen. The reaction is complete in 15 min at 37 degrees C. The standard curve is linear up to a urea concentration of 40 mmol/L. Precision is good; CVs ranged from 2.5% to 3.1%. Results by the present method compared well with those by a candidate Reference Method and are not subject to interferences from commonly used drugs and anticoagulants.


The following articles in journals at HighWire Press have cited this article:


Home page
 Clin. Chem.Home page
B. Naslund, L. Stahle, A. Lundin, B. Anderstam, P. Arner, and J. Bergstrom
Luminometric single step urea assay using ATP-hydrolyzing urease
Clin. Chem., September 1, 1998; 44(9): 1964 - 1973.
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Copyright © 1989 by the American Association for Clinical Chemistry.