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Identification of a glutathione S-transferase without affinity for glutathione sepharose in human kidney

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Summary.

To identify kidney glutathione S-transferase (GST) isoenzyme, which does not bind to glutathione affinity column, biochemical characterization was performed by using an array of substrates and by measuring sensitivity to inhibitors. Immunological characterization was done by immunoblotting. Affinity flow-through GST exhibited activity towards 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole and cumene hydroperoxide, typical class α substrates and high sensitivity towards hematin, an α class inhibitor. It cross-reacted with antibodies against α class GST. Affinity flow-through GST in human kidney is an α class member.

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Authors and Affiliations

  1. Institute of Biochemistry, Belgrade University School of Medicine, Belgrade, Serbia and Montenegro

    T. Simic, M. Pljesa-Ercegovac, A. Savic-Radojevic, M. Hadziahmetovic & J. Mimic-Oka

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  1. T. Simic
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  2. M. Pljesa-Ercegovac
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  3. A. Savic-Radojevic
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  4. M. Hadziahmetovic
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  5. J. Mimic-Oka
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Simic, T., Pljesa-Ercegovac, M., Savic-Radojevic, A. et al. Identification of a glutathione S-transferase without affinity for glutathione sepharose in human kidney. Amino Acids 30, 495–498 (2006). https://doi.org/10.1007/s00726-006-0329-7

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  • DOI: https://doi.org/10.1007/s00726-006-0329-7

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