Cationic glutathione S-transferase of human erythrocytes has unique kinetic characteristics among human glutathione S-transferases |
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| Authors: | S V Singh Y C Awasthi |
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| Affiliation: | 1. Division of Membrane Physiology, Department of Cell Physiology, National Institute for Physiological Sciences, National Institutes of Natural Sciences, Okazaki, Japan;2. Department of Physiological Sciences, School of Life Science, SOKENDAI (The Graduate University for Advanced Studies), Okazaki, Japan;1. Infinitus (China) Company Limited, Jiangmen 528156, Guangdong, People''s Republic of China;2. School of Perfume and Aroma Technology, Shanghai Institute of Technology, No.100, Haiquan Road, Fengxian district, Shanghai 201418, People''s Republic of China;3. Shanghai Jointvace Company Limited, Shanghai 200062, People''s Republic of China;1. Department of Psychology, The Chinese University of Hong Kong, Hong Kong;2. Western Sydney University, NICM Heath Research Institute, Westmead, NSW, Australia;3. Professorial Unit, The Melbourne Clinic, Department of Psychiatry, The University of Melbourne, VIC, Australia;4. Department of Psychiatry, The Melbourne Clinic and St Vincent''s Hospital, The University of Melbourne, Richmond, VIC, Australia |
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| Abstract: | The cationic glutathione S-transferase (GST sigma) of human erythrocytes is activated when incubated with 1 mM N-ethylmaleimide or other sulfhydryl blocking agents. Other GST isoenzymes of human tissues were inhibited by these reagents under similar conditions. At higher concentrations of NEM, GST sigma was also inhibited. Dithiothreitol, 2-mercaptoethanol, and sodium borohydride also caused several fold activation of GST sigma but noe of the other human GST isoenzymes were activated by these reagents. |
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