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Glutathione‐S‐transferase activity in malarial parasites
Author(s) -
Srivastava P.,
Puri S. K.,
Kamboj K. K.,
Pandey V. C.
Publication year - 1999
Publication title -
tropical medicine and international health
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.056
H-Index - 114
eISSN - 1365-3156
pISSN - 1360-2276
DOI - 10.1046/j.1365-3156.1999.00387.x
Subject(s) - plasmodium knowlesi , plasmodium berghei , hemin , chloroquine , glutathione , glutathione s transferase , biology , plasmodium yoelii , plasmodium falciparum , enzyme , malaria , virology , pharmacology , biochemistry , plasmodium vivax , heme , parasitemia , immunology
Summary Glutathione‐S‐transferase (GST) activity has been detected in rodent ( Plasmodium berghei, P. yoelii ), simian ( P. knowlesi ) and human ( P. falciparum ) malarial parasites, and in different intraerythrocytic stages of P. knowlesi (schizont > ring > trophozoite). In chloroquine‐resistant strains of rodent and human malarial parasites GST activity significantly increases compared to sensitive strains. Further, the increase in enzyme activity is directly related to drug pressure of resistant P. berghei . Complete inhibition of chloroquine‐sensitive and resistant P. berghei glutathione‐S‐transferase activities was observed at 2.5 and 5.0 μm concentration of hemin, respectively. An inverse relationship was found between the heme level and enzyme activity of chloroquine‐resistant and sensitive P. berghei . Chloroquine, artemisinin, and primaquine noticeably inhibited GST activity in P. knowlesi .