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Clinical Chemistry 18: 523-527, 1972;
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Clinical Chemistry, Vol 18, 523-527, Copyright © 1972 by the American Association for Clinical Chemistry

Optimal Conditions for the Kinetic Assay of Serum Glutamate Dehydrogenase Activity at 37°C

Graham Ellis 1 and David M. Goldberg 1

1 Department of Chemical Pathology, Royal Hospital, West St., Sheffield S1 3SR, U.K.

Optimal concentrations of ammonium ions, 2-oxoglutarate, and NADH were defined for serum glutamate dehydrogenase (EC 1.4.1.2) activity at 37°C. Substrate inhibition was not observed with the last two compounds. The pH optimum in triethanolamine buffer is 7.4, and activity is inhibited by increasing the buffer concentration beyond 50 mmol/liter. Activation by ADP exceeds that promoted by L-leucine, and there is little advantage in having both present. Activity is linear with time and with enzyme concentration to a limiting absorbance change of 0.300 at 340 nm, and precision was satisfactory. Data indicate the normal range to lie between 0 and 4 U/liter.


Key Words: factors affecting the analysis • normal range • enzyme activation • spectrophotometric assay • ionic strength • substrate inhibition • enzyme stability

Submitted on February 24, 1972
Accepted on March 28, 1972




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