Adaptation of a γ-glutamyl transpeptidase assay to microtiter plates

Paul M. Silber, A. Jay Gandolfi, Klaus Brendel

Research output: Contribution to journalArticle

23 Scopus citations

Abstract

A kinetic assay for measuring γ-glutamyl transpeptidase (GGT) activity has been adapted to microtiter plates and an automated microtiter plate reader. This method permits the simultaneous analysis of enzyme activity in a large number of samples incubated with the chromogenic GGT substrate γ-glutamyl-p-nitroanilide. A major advantage of this assay over previously reported methods is the substantial reduction in the time needed for measuring sample enzyme activity. In addition, reduction of the total assay volume to 0.28 ml conserves both sample and reagents. This method has been calibrated at 23°C using purified GGT, and used to analyze GGT activity in human sera. The assay is sensitive over a range of 3-200 U/liter.

Original languageEnglish (US)
Pages (from-to)68-71
Number of pages4
JournalAnalytical Biochemistry
Volume158
Issue number1
DOIs
StatePublished - Oct 1986

Keywords

  • automated spectrophotometry
  • clinical chemistry
  • enzymatic assay
  • enzyme
  • kinetics
  • microtiter plates
  • γ-glutamyl transpeptidase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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