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In-Vitro Inhibition of Camel Hepatic Glutathione Transferase by Quercetin

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), 2014. 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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[10] Raza H, John A, Lakhani MS, Ahmed I, Montague W. Multiplicity and tissue specific expression of camel cytochrome P450(s). Comp Biochem Physiol C Pharmacol Toxicol Endocrinol. 1998;121(1-3):205-11.
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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
  • Dept. of Biochemistry, King Saud University, Riyadh 11495, Saudi Arabia

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

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

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