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Clinical Chemistry 20: 1121-1124, 1974;
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Clinical Chemistry, Vol 20, 1121-1124, Copyright © 1974 by the American Association for Clinical Chemistry

Optimized Determination of ggr-Glutamyltransferase by Reaction-Rate Analysis

Sidney B. Rosalki 1 and David Tarlow 1

1 Department of Diagnostic Chemical Pathology, St. Mary’s Hospital, London, W.2., England.

We describe a method for measuring ggr-glutamyltransferase (EC 2.3.2.2) activity in serum, which can be used with automated enzyme analyzers (such as the LKB 8600 Reaction Rate Analyzer) that require enzyme reactions to be initiated with substrate. The method also permits optimal determination conditions to be obtained at 37 °C. The enzymatic reaction is commenced by adding ggr-glutamyl-p-nitroanilide dissolved in dilute hydrochloric acid to samples pre-incubated with tris(hydroxymethyl)aminomethane—glycylglycine buffer. The p-nitroaniline liberated is continously monitored at 37 °C at 405 nm. The pH of the pre-incubation buffer is such that the optimal pH for the enzyme reaction results from addition of the acid substrate solution.


Key Words: LKB Analyzer • liver disease • kinetic enzyme assay

Submitted on March 19, 1974
Accepted on May 29, 1974




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Gamma Glutamyl Transferase and Metabolic Syndrome, Cardiovascular Disease, and Mortality Risk: The Framingham Heart Study
Arterioscler. Thromb. Vasc. Biol., January 1, 2007; 27(1): 127 - 133.
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