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Purification and characterisation of the soluble glutathione S‐transferase isoenzymes in rat kidney derived NRK cells
Author(s) -
Dierickx Paul J.,
Noble Elisabeth
Publication year - 1997
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549700202081
Subject(s) - chromatofocusing , kidney , isozyme , glutathione , glutathione s transferase , enzyme , biochemistry , chemistry , in vitro , microbiology and biotechnology , biology , endocrinology , isoelectric point
Glutathione S‐transferase (GST) enzymes are toxicologically important from many points of view. Rat kidney derived established NRK cells were mass cultured for the isolation of GST isoenzymes. These were enriched by affinity chromatography and separated by chromatofocusing and HPLC. Exactly the same major GST subunits were found in NRK cells as in the rat kidney. Strong evidence was also found for the presence of an aberrant form of GST 7‐7, as was described in rat kidney. A very good correlation between the NRK GST and rat kidney, and especially cis‐platinum treated kidney, was found. It is concluded that NRK cells can be considered as a valuable alternative tool for in vitro research of rat kidney phenomena, especially when toxicological interactions are investigated.