Journal of Plant Sciences

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Comparative Investigation of Glutathione S-transferase (GST) in Different Crops and Purification of High Active GSTs from Onion (Allium cepa L.)

Received: 18 May 2015    Accepted: 25 May 2015    Published: 13 June 2015
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Abstract

Glutathione S-transferases (GSTs; EC 2.5.1.18) are abundant proteins encoded by a highly divergent ancient gene family with protective functions through detoxification and non-catalytic roles as carriers of cytotoxins. In this work, we investigated the GST activities in seedlings of 38 crops to obtain a plant with high active GST for further study. In screening of 38 crops, onion seedling showed the highest GST activity (483.54 nmol min-1mg-1 protein) followed by wheat(372.89 nmol min-1mg-1 protein), barley (253.44 nmol min-1mg-1 protein), rice (244.12 nmol min-1mg-1 protein) and proso millet (173.34 nmol min-1mg-1 protein). Carrot seedling showed the lowest activity (3.63 nmol min-1mg-1 protein).In onion plants, both root and leaf showed high GST activity. Onion bulb GSTs were separated DEAE cellulose column chromatography, and purified by affinity chromatography (S-hexyl glutathione-agarose). Three GST peaks were found to elute at 67, 107 and 140mM of KCl gradient solution, and were named as GSTa, GSTb and GSTc. Among the three GSTs, GSTa, GSTb and GSTc contained 9.58, 61.45 and 28.97% of total activity, respectively. In purification, GSTa, GSTb and GSTc had specific activities of 9075, 17259 and 19868 nmol min-1 mg-1 protein, respectively, along with yield of 2.48, 3.17 and 1.28,and purification fold of 15.8, 29.9 and 34.5, respectively. The purity and molecular mass of the fraction was examined by SDS-PAGE. The silver staining of the purified GSTa, GSTb and GSTc indicated that final product of GSTb and GSTc were highly purified and migrated as a single band on SDS-PAGE with an apparent molecular mass of 27 kDa. However, GSTa eluted with Glyoxalase-I (Gly-I) and to purify GSTa, more methodological application are suggested.

DOI 10.11648/j.jps.20150303.17
Published in Journal of Plant Sciences (Volume 3, Issue 3, June 2015)
Page(s) 162-170
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

Comparative GST, Crops, Purification, High Active GST, Onion

References
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Author Information
  • Molecular Breeding Lab, Bangladesh Agricultural Research Institute, Gazipur, Bangladesh; Department of Genetics and Plant Breeding, Patuakhali Science and Technology University, Patuakhali, Bangladesh

  • Department of Genetics and Plant Breeding, Patuakhali Science and Technology University, Patuakhali, Bangladesh

  • Molecular Breeding Lab, Bangladesh Agricultural Research Institute, Gazipur, Bangladesh

  • Molecular Breeding Lab, Bangladesh Agricultural Research Institute, Gazipur, Bangladesh

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    Md. Raisul Islam, Abul Kashem Chowdhury, Md. Mahfuzur Rahman, Md. Motiar Rohman. (2015). Comparative Investigation of Glutathione S-transferase (GST) in Different Crops and Purification of High Active GSTs from Onion (Allium cepa L.). Journal of Plant Sciences, 3(3), 162-170. https://doi.org/10.11648/j.jps.20150303.17

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    Md. Raisul Islam; Abul Kashem Chowdhury; Md. Mahfuzur Rahman; Md. Motiar Rohman. Comparative Investigation of Glutathione S-transferase (GST) in Different Crops and Purification of High Active GSTs from Onion (Allium cepa L.). J. Plant Sci. 2015, 3(3), 162-170. doi: 10.11648/j.jps.20150303.17

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    AMA Style

    Md. Raisul Islam, Abul Kashem Chowdhury, Md. Mahfuzur Rahman, Md. Motiar Rohman. Comparative Investigation of Glutathione S-transferase (GST) in Different Crops and Purification of High Active GSTs from Onion (Allium cepa L.). J Plant Sci. 2015;3(3):162-170. doi: 10.11648/j.jps.20150303.17

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  • @article{10.11648/j.jps.20150303.17,
      author = {Md. Raisul Islam and Abul Kashem Chowdhury and Md. Mahfuzur Rahman and Md. Motiar Rohman},
      title = {Comparative Investigation of Glutathione S-transferase (GST) in Different Crops and Purification of High Active GSTs from Onion (Allium cepa L.)},
      journal = {Journal of Plant Sciences},
      volume = {3},
      number = {3},
      pages = {162-170},
      doi = {10.11648/j.jps.20150303.17},
      url = {https://doi.org/10.11648/j.jps.20150303.17},
      eprint = {https://download.sciencepg.com/pdf/10.11648.j.jps.20150303.17},
      abstract = {Glutathione S-transferases (GSTs; EC 2.5.1.18) are abundant proteins encoded by a highly divergent ancient gene family with protective functions through detoxification and non-catalytic roles as carriers of cytotoxins. In this work, we investigated the GST activities in seedlings of 38 crops to obtain a plant with high active GST for further study. In screening of 38 crops, onion seedling showed the highest GST activity (483.54 nmol min-1mg-1 protein) followed by wheat(372.89 nmol min-1mg-1 protein), barley (253.44 nmol min-1mg-1 protein), rice (244.12 nmol min-1mg-1 protein) and proso millet (173.34 nmol min-1mg-1 protein). Carrot seedling showed the lowest activity (3.63 nmol min-1mg-1 protein).In onion plants, both root and leaf showed high GST activity. Onion bulb GSTs were separated DEAE cellulose column chromatography, and purified by affinity chromatography (S-hexyl glutathione-agarose). Three GST peaks were found to elute at 67, 107 and 140mM of KCl gradient solution, and were named as GSTa, GSTb and GSTc. Among the three GSTs, GSTa, GSTb and GSTc contained 9.58, 61.45 and 28.97% of total activity, respectively. In purification, GSTa, GSTb and GSTc had specific activities of 9075, 17259 and 19868 nmol min-1 mg-1 protein, respectively, along with yield of 2.48, 3.17 and 1.28,and purification fold of 15.8, 29.9 and 34.5, respectively. The purity and molecular mass of the fraction was examined by SDS-PAGE. The silver staining of the purified GSTa, GSTb and GSTc indicated that final product of GSTb and GSTc were highly purified and migrated as a single band on SDS-PAGE with an apparent molecular mass of 27 kDa. However, GSTa eluted with Glyoxalase-I (Gly-I) and to purify GSTa, more methodological application are suggested.},
     year = {2015}
    }
    

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  • TY  - JOUR
    T1  - Comparative Investigation of Glutathione S-transferase (GST) in Different Crops and Purification of High Active GSTs from Onion (Allium cepa L.)
    AU  - Md. Raisul Islam
    AU  - Abul Kashem Chowdhury
    AU  - Md. Mahfuzur Rahman
    AU  - Md. Motiar Rohman
    Y1  - 2015/06/13
    PY  - 2015
    N1  - https://doi.org/10.11648/j.jps.20150303.17
    DO  - 10.11648/j.jps.20150303.17
    T2  - Journal of Plant Sciences
    JF  - Journal of Plant Sciences
    JO  - Journal of Plant Sciences
    SP  - 162
    EP  - 170
    PB  - Science Publishing Group
    SN  - 2331-0731
    UR  - https://doi.org/10.11648/j.jps.20150303.17
    AB  - Glutathione S-transferases (GSTs; EC 2.5.1.18) are abundant proteins encoded by a highly divergent ancient gene family with protective functions through detoxification and non-catalytic roles as carriers of cytotoxins. In this work, we investigated the GST activities in seedlings of 38 crops to obtain a plant with high active GST for further study. In screening of 38 crops, onion seedling showed the highest GST activity (483.54 nmol min-1mg-1 protein) followed by wheat(372.89 nmol min-1mg-1 protein), barley (253.44 nmol min-1mg-1 protein), rice (244.12 nmol min-1mg-1 protein) and proso millet (173.34 nmol min-1mg-1 protein). Carrot seedling showed the lowest activity (3.63 nmol min-1mg-1 protein).In onion plants, both root and leaf showed high GST activity. Onion bulb GSTs were separated DEAE cellulose column chromatography, and purified by affinity chromatography (S-hexyl glutathione-agarose). Three GST peaks were found to elute at 67, 107 and 140mM of KCl gradient solution, and were named as GSTa, GSTb and GSTc. Among the three GSTs, GSTa, GSTb and GSTc contained 9.58, 61.45 and 28.97% of total activity, respectively. In purification, GSTa, GSTb and GSTc had specific activities of 9075, 17259 and 19868 nmol min-1 mg-1 protein, respectively, along with yield of 2.48, 3.17 and 1.28,and purification fold of 15.8, 29.9 and 34.5, respectively. The purity and molecular mass of the fraction was examined by SDS-PAGE. The silver staining of the purified GSTa, GSTb and GSTc indicated that final product of GSTb and GSTc were highly purified and migrated as a single band on SDS-PAGE with an apparent molecular mass of 27 kDa. However, GSTa eluted with Glyoxalase-I (Gly-I) and to purify GSTa, more methodological application are suggested.
    VL  - 3
    IS  - 3
    ER  - 

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