In-Vitro Inhibition of Camel Hepatic Glutathione Transferase by Quercetin

Ghada Al-Amro; Mohammad Ali Qorban; Samina Hyder Haq

doi:doi:10.11648/j.ab.20140205.13

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In-Vitro Inhibition of Camel Hepatic Glutathione Transferase by Quercetin

Ghada Al-Amro, Mohammad Ali Qorban, Samina Hyder Haq

Published in Advances in Biochemistry (Volume 2, Issue 5)

Received: 7 September 2014 Accepted: 19 September 2014 Published: 30 October 2014

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Abstract

Glutathione S-transferases (GST) are a group of multifunctional ubiquitous enzymes widely present in animals and plants, which catalysis the conjugation of glutathione to different exogenous and endogenous electrophilic compounds. This study was carried out to characterize the purified GST enzyme from camel liver tissues and to investigate the in-vitro inhibitory effect of the flavonoid quercetin by measuring S-2,4-dinitrophenyl glutathione (DNP-GSH) formation from 1-chloro-2,4-dinitrobenzene (CDNB) and reduced glutathione(GSH) as substrates. The Km values for reduced GSH and CDNB were found to be 0.08438 and 0.6827 mM while Vmax values were 6.935 and 15.599 mM/min respectively. The IC50 was determined to be 1.8 mM. The inhibition constant (Ki) was estimated to be 1.91 mM at 0.5 mM and 1.76 mM at 2 mM. The mean inhibition constant (Ki) was estimated to be 1.835±0.075mM which revealed an uncompetitive profile and indicated quercetin as a weak inhibitor with the varied concentration of CDNB and fixed concentration of reduced GSH as a substrate.

Published in	Advances in Biochemistry (Volume 2, Issue 5)
DOI	10.11648/j.ab.20140205.13
Page(s)	71-75
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

GST, Glutathione S-Transferase, CDNB, 1-Chloro-2,4-Dinitrobenzene, (Vmaxapp), Apparent Vmax, (IC50), The Inhibitor Concentration Causing 50% Inhibition, Km, Michaelis Constant, (Ki), Inhibitor Constant, (Kmapp), Apparent Km

References

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[16]	van Zanden JJ, Ben Hamman O, van Iersel ML, Boeren S, Cnubben NH, Lo Bello M, et al. Inhibition of human glutathione S-transferase P1-1 by the flavonoid quercetin. Chem Biol Interact. 2003;145(2):139-48.
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APA Style

Ghada Al-Amro, Mohammad Ali Qorban, Samina Hyder Haq. (2014). In-Vitro Inhibition of Camel Hepatic Glutathione Transferase by Quercetin. Advances in Biochemistry, 2(5), 71-75. https://doi.org/10.11648/j.ab.20140205.13

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ACS Style

Ghada Al-Amro; Mohammad Ali Qorban; Samina Hyder Haq. In-Vitro Inhibition of Camel Hepatic Glutathione Transferase by Quercetin. Adv. Biochem. 2014, 2(5), 71-75. doi: 10.11648/j.ab.20140205.13

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AMA Style

Ghada Al-Amro, Mohammad Ali Qorban, Samina Hyder Haq. In-Vitro Inhibition of Camel Hepatic Glutathione Transferase by Quercetin. Adv Biochem. 2014;2(5):71-75. doi: 10.11648/j.ab.20140205.13

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@article{10.11648/j.ab.20140205.13,
  author = {Ghada Al-Amro and Mohammad Ali Qorban and Samina Hyder Haq},
  title = {In-Vitro Inhibition of Camel Hepatic Glutathione Transferase by Quercetin},
  journal = {Advances in Biochemistry},
  volume = {2},
  number = {5},
  pages = {71-75},
  doi = {10.11648/j.ab.20140205.13},
  url = {https://doi.org/10.11648/j.ab.20140205.13},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ab.20140205.13},
  abstract = {Glutathione S-transferases (GST) are a group of multifunctional ubiquitous enzymes widely present in animals and plants, which catalysis the conjugation of glutathione to different exogenous and endogenous electrophilic compounds. This study was carried out to characterize the purified GST enzyme from camel liver tissues and to investigate the in-vitro inhibitory effect of the flavonoid quercetin by measuring S-2,4-dinitrophenyl glutathione (DNP-GSH) formation from 1-chloro-2,4-dinitrobenzene (CDNB) and reduced glutathione(GSH) as substrates. The Km values for reduced GSH and CDNB were found to be 0.08438 and 0.6827 mM while Vmax values were 6.935 and 15.599 mM/min respectively. The IC50 was determined to be 1.8 mM. The inhibition constant (Ki) was estimated to be 1.91 mM at 0.5 mM and 1.76 mM at 2 mM. The mean inhibition constant (Ki) was estimated to be 1.835±0.075mM which revealed an uncompetitive profile and indicated quercetin as a weak inhibitor with the varied concentration of CDNB and fixed concentration of reduced GSH as a substrate.},
 year = {2014}
}

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TY  - JOUR
T1  - In-Vitro Inhibition of Camel Hepatic Glutathione Transferase by Quercetin
AU  - Ghada Al-Amro
AU  - Mohammad Ali Qorban
AU  - Samina Hyder Haq
Y1  - 2014/10/30
PY  - 2014
N1  - https://doi.org/10.11648/j.ab.20140205.13
DO  - 10.11648/j.ab.20140205.13
T2  - Advances in Biochemistry
JF  - Advances in Biochemistry
JO  - Advances in Biochemistry
SP  - 71
EP  - 75
PB  - Science Publishing Group
SN  - 2329-0862
UR  - https://doi.org/10.11648/j.ab.20140205.13
AB  - Glutathione S-transferases (GST) are a group of multifunctional ubiquitous enzymes widely present in animals and plants, which catalysis the conjugation of glutathione to different exogenous and endogenous electrophilic compounds. This study was carried out to characterize the purified GST enzyme from camel liver tissues and to investigate the in-vitro inhibitory effect of the flavonoid quercetin by measuring S-2,4-dinitrophenyl glutathione (DNP-GSH) formation from 1-chloro-2,4-dinitrobenzene (CDNB) and reduced glutathione(GSH) as substrates. The Km values for reduced GSH and CDNB were found to be 0.08438 and 0.6827 mM while Vmax values were 6.935 and 15.599 mM/min respectively. The IC50 was determined to be 1.8 mM. The inhibition constant (Ki) was estimated to be 1.91 mM at 0.5 mM and 1.76 mM at 2 mM. The mean inhibition constant (Ki) was estimated to be 1.835±0.075mM which revealed an uncompetitive profile and indicated quercetin as a weak inhibitor with the varied concentration of CDNB and fixed concentration of reduced GSH as a substrate.
VL  - 2
IS  - 5
ER  -

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Author Information

Ghada Al-Amro

Dept. of Biochemistry, King Saud University, Riyadh 11495, Saudi Arabia
Mohammad Ali Qorban

Dept. of Biochemistry, King Saud University, Riyadh 11495, Saudi Arabia
Samina Hyder Haq

Dept. of Biochemistry, King Saud University, Riyadh 11495, Saudi Arabia

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Plain Text BibTeX RIS

APA Style

Ghada Al-Amro, Mohammad Ali Qorban, Samina Hyder Haq. (2014). In-Vitro Inhibition of Camel Hepatic Glutathione Transferase by Quercetin. Advances in Biochemistry, 2(5), 71-75. https://doi.org/10.11648/j.ab.20140205.13

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ACS Style

Ghada Al-Amro; Mohammad Ali Qorban; Samina Hyder Haq. In-Vitro Inhibition of Camel Hepatic Glutathione Transferase by Quercetin. Adv. Biochem. 2014, 2(5), 71-75. doi: 10.11648/j.ab.20140205.13

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AMA Style

Ghada Al-Amro, Mohammad Ali Qorban, Samina Hyder Haq. In-Vitro Inhibition of Camel Hepatic Glutathione Transferase by Quercetin. Adv Biochem. 2014;2(5):71-75. doi: 10.11648/j.ab.20140205.13

Copy | Download

@article{10.11648/j.ab.20140205.13,
  author = {Ghada Al-Amro and Mohammad Ali Qorban and Samina Hyder Haq},
  title = {In-Vitro Inhibition of Camel Hepatic Glutathione Transferase by Quercetin},
  journal = {Advances in Biochemistry},
  volume = {2},
  number = {5},
  pages = {71-75},
  doi = {10.11648/j.ab.20140205.13},
  url = {https://doi.org/10.11648/j.ab.20140205.13},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ab.20140205.13},
  abstract = {Glutathione S-transferases (GST) are a group of multifunctional ubiquitous enzymes widely present in animals and plants, which catalysis the conjugation of glutathione to different exogenous and endogenous electrophilic compounds. This study was carried out to characterize the purified GST enzyme from camel liver tissues and to investigate the in-vitro inhibitory effect of the flavonoid quercetin by measuring S-2,4-dinitrophenyl glutathione (DNP-GSH) formation from 1-chloro-2,4-dinitrobenzene (CDNB) and reduced glutathione(GSH) as substrates. The Km values for reduced GSH and CDNB were found to be 0.08438 and 0.6827 mM while Vmax values were 6.935 and 15.599 mM/min respectively. The IC50 was determined to be 1.8 mM. The inhibition constant (Ki) was estimated to be 1.91 mM at 0.5 mM and 1.76 mM at 2 mM. The mean inhibition constant (Ki) was estimated to be 1.835±0.075mM which revealed an uncompetitive profile and indicated quercetin as a weak inhibitor with the varied concentration of CDNB and fixed concentration of reduced GSH as a substrate.},
 year = {2014}
}

Copy | Download

TY  - JOUR
T1  - In-Vitro Inhibition of Camel Hepatic Glutathione Transferase by Quercetin
AU  - Ghada Al-Amro
AU  - Mohammad Ali Qorban
AU  - Samina Hyder Haq
Y1  - 2014/10/30
PY  - 2014
N1  - https://doi.org/10.11648/j.ab.20140205.13
DO  - 10.11648/j.ab.20140205.13
T2  - Advances in Biochemistry
JF  - Advances in Biochemistry
JO  - Advances in Biochemistry
SP  - 71
EP  - 75
PB  - Science Publishing Group
SN  - 2329-0862
UR  - https://doi.org/10.11648/j.ab.20140205.13
AB  - Glutathione S-transferases (GST) are a group of multifunctional ubiquitous enzymes widely present in animals and plants, which catalysis the conjugation of glutathione to different exogenous and endogenous electrophilic compounds. This study was carried out to characterize the purified GST enzyme from camel liver tissues and to investigate the in-vitro inhibitory effect of the flavonoid quercetin by measuring S-2,4-dinitrophenyl glutathione (DNP-GSH) formation from 1-chloro-2,4-dinitrobenzene (CDNB) and reduced glutathione(GSH) as substrates. The Km values for reduced GSH and CDNB were found to be 0.08438 and 0.6827 mM while Vmax values were 6.935 and 15.599 mM/min respectively. The IC50 was determined to be 1.8 mM. The inhibition constant (Ki) was estimated to be 1.91 mM at 0.5 mM and 1.76 mM at 2 mM. The mean inhibition constant (Ki) was estimated to be 1.835±0.075mM which revealed an uncompetitive profile and indicated quercetin as a weak inhibitor with the varied concentration of CDNB and fixed concentration of reduced GSH as a substrate.
VL  - 2
IS  - 5
ER  -

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