CLC number: R446
On-line Access: 2011-03-09
Received: 2010-05-10
Revision Accepted: 2010-07-23
Crosschecked: 2011-01-25
Cited: 5
Clicked: 4915
Zhi-rong Li, Yin Liu, Xiao-lan Yang, Jun Pu, Bei-zhong Liu, Yong-hua Yuan, Yan-ling Xie, Fei Liao. Kinetic analysis of γ-glutamyltransferase reaction process for measuring activity via an integration strategy at low concentrations of γ-glutamyl p-nitroaniline[J]. Journal of Zhejiang University Science B, 2011, 12(3): 180-188.
@article{title="Kinetic analysis of γ-glutamyltransferase reaction process for measuring activity via an integration strategy at low concentrations of γ-glutamyl p-nitroaniline",
author="Zhi-rong Li, Yin Liu, Xiao-lan Yang, Jun Pu, Bei-zhong Liu, Yong-hua Yuan, Yan-ling Xie, Fei Liao",
journal="Journal of Zhejiang University Science B",
volume="12",
number="3",
pages="180-188",
year="2011",
publisher="Zhejiang University Press & Springer",
doi="10.1631/jzus.B1000171"
}
%0 Journal Article
%T Kinetic analysis of γ-glutamyltransferase reaction process for measuring activity via an integration strategy at low concentrations of γ-glutamyl p-nitroaniline
%A Zhi-rong Li
%A Yin Liu
%A Xiao-lan Yang
%A Jun Pu
%A Bei-zhong Liu
%A Yong-hua Yuan
%A Yan-ling Xie
%A Fei Liao
%J Journal of Zhejiang University SCIENCE B
%V 12
%N 3
%P 180-188
%@ 1673-1581
%D 2011
%I Zhejiang University Press & Springer
%DOI 10.1631/jzus.B1000171
TY - JOUR
T1 - Kinetic analysis of γ-glutamyltransferase reaction process for measuring activity via an integration strategy at low concentrations of γ-glutamyl p-nitroaniline
A1 - Zhi-rong Li
A1 - Yin Liu
A1 - Xiao-lan Yang
A1 - Jun Pu
A1 - Bei-zhong Liu
A1 - Yong-hua Yuan
A1 - Yan-ling Xie
A1 - Fei Liao
J0 - Journal of Zhejiang University Science B
VL - 12
IS - 3
SP - 180
EP - 188
%@ 1673-1581
Y1 - 2011
PB - Zhejiang University Press & Springer
ER -
DOI - 10.1631/jzus.B1000171
Abstract: At 0.12 mmol/L γ;-glutamyl p-nitroaniline (GGPNA), an improved integrated method was developed for kinetic analysis of γ;-Glutamyltransferase (GGT) reaction process and the integration with the classical initial rate method to measure serum GGT. For the improved integrated method, an integrated rate equation, which used the predictor variable of reaction time and considered inhibitions by both GGPNA and products, was nonlinearly fit to GGT reaction processes. For the integration strategy, classical initial rates were estimated when GGPNA consumption percentages were below 50%; otherwise, maximal reaction rates of GGT were estimated by the improved integrated method and converted into initial rates according to the differential rate equation at 0.11 mmol/L GGPNA. The integration strategy was validated using optimized GGT kinetic parameters and 10-s intervals to record reaction curves within 8.0 min. By the integration strategy, there was a linear response from 0.9 to 32.0 U/L GGT, coefficients of variation were below 3.5% for GGT from 8.0 to 32.0 U/L (n=5), and GGT activities in clinical sera responded linearly to their classical initial rates at 2.00 mmol/L GGPNA with an expected slope. Therefore, the integration strategy was successful in measuring GGT at 0.12 mmol/L GGPNA.
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