Glutathione S-transferases from the gastrointestinal nematode Heligmosomoides polygyrus and mammalian liver compared |
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Institution: | 1. Section of Parasitology, Department of Zoology, Aligarh Muslim University, Aligarh, India;2. Department of Zoology, School of Biosciences and Biotechnology, BGSB University, Jammu and Kashmir, India;1. Department of Orthopaedic Surgery, Ilsan Paik Hospital, Inje University School of Medicine, Goyangsi, Gyeonggido, Republic of Korea;2. Department of Orthopaedic Surgery, Bareunsesang Hospital, Bundangsi, Gyeonggido, Republic of Korea;3. Department of Orthopaedic Surgery, National Medical Center, Seoul, Republic of Korea;4. Department of Orthopaedic Surgery, Samsung Medical Center, Sungkyunkwan University School of Medicine, Seoul, Republic of Korea;5. Department of Orthopaedic Surgery, Gil Medical Center, Gacheon University School of Medicine, Incheon, Republic of Korea;6. Department of Pathology, Keimyung University School of Medicine, Daegu, Republic of Korea;7. Department of Orthopaedic Surgery, Samsung Medical Center, Sungkyunkwan University School of Medicine, Seoul, Republic of Korea;8. Department of Health Sciences and Technology and Department of Medical Device Management and Research, SAIHST, Sungkyunkwan University, Seoul, Republic of Korea |
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Abstract: | Glutathione S-transferases have been partially characterised from the gastrointestinal nematode Heligmosomoides polygyrus. Two major subunit families were purified (24 and 23 kDa) with N-terminal homology to the mammalian Alpha family. Four dimeric forms of GST were purified from the nematode by glutathione-affinity chromatography, two major enzymes (pI 8.1, 5.0) and two minor forms (pI 5.8, 5.3). The purified GST pool could neutralize model and lipid peroxides via peroxidase activity but not peroxidation derived reactive carbonyls via glutathione transferase activity. Antisera raised to the pooled nematode GSTs appeared to recognize other Strongylida GSTs more strongly on Western blotting compared to mammalian GSTs. |
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