Adaptation of a γ-glutamyl transpeptidase assay to microtiter plates

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

doi:10.1016/0003-2697(86)90590-7

Adaptation of a γ-glutamyl transpeptidase assay to microtiter plates

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

Research output: Contribution to journal › Article › peer-review

26 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 language	English (US)
Pages (from-to)	68-71
Number of pages	4
Journal	Analytical Biochemistry
Volume	158
Issue number	1
DOIs	https://doi.org/10.1016/0003-2697(86)90590-7
State	Published - 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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@article{76d62ad4d7634931a5b31d03400f2011,

title = "Adaptation of a γ-glutamyl transpeptidase assay to microtiter plates",

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.",

keywords = "automated spectrophotometry, clinical chemistry, enzymatic assay, enzyme, kinetics, microtiter plates, γ-glutamyl transpeptidase",

author = "Silber, {Paul M.} and Gandolfi, {A. Jay} and Klaus Brendel",

note = "Funding Information: {\textquoteright} Supported by NIEHS Training Grant T32ES0709 1. 2 Abbreviations used: GGT, y-glutamyl transpeptidase; GPNA, y-glutamyl-pnitroanilide; pNA, pnitroaniline.",

year = "1986",

month = oct,

doi = "10.1016/0003-2697(86)90590-7",

language = "English (US)",

volume = "158",

pages = "68--71",

journal = "Analytical Biochemistry",

issn = "0003-2697",

publisher = "Academic Press Inc.",

number = "1",

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TY - JOUR

T1 - Adaptation of a γ-glutamyl transpeptidase assay to microtiter plates

AU - Silber, Paul M.

AU - Gandolfi, A. Jay

AU - Brendel, Klaus

N1 - Funding Information: ’ Supported by NIEHS Training Grant T32ES0709 1. 2 Abbreviations used: GGT, y-glutamyl transpeptidase; GPNA, y-glutamyl-pnitroanilide; pNA, pnitroaniline.

PY - 1986/10

Y1 - 1986/10

N2 - 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.

AB - 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.

KW - automated spectrophotometry

KW - clinical chemistry

KW - enzymatic assay

KW - enzyme

KW - kinetics

KW - microtiter plates

KW - γ-glutamyl transpeptidase

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U2 - 10.1016/0003-2697(86)90590-7

DO - 10.1016/0003-2697(86)90590-7

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C2 - 2879485

AN - SCOPUS:0023002608

SN - 0003-2697

VL - 158

SP - 68

EP - 71

JO - Analytical Biochemistry

JF - Analytical Biochemistry

IS - 1

ER -

Adaptation of a γ-glutamyl transpeptidase assay to microtiter plates

Abstract

Keywords

ASJC Scopus subject areas

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