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Comparative Studies on Dihydrofolate Reductases from Plasmodium falciparum and Aotus trivirgatus *
Author(s) -
KAN S. C.,
SIDDIQUI W. A.
Publication year - 1979
Publication title -
the journal of protozoology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 0022-3921
DOI - 10.1111/j.1550-7408.1979.tb04216.x
Subject(s) - dihydrofolate reductase , plasmodium falciparum , enzyme , biology , parasite hosting , pyrimethamine , host (biology) , enzyme assay , biochemistry , virology , malaria , immunology , genetics , world wide web , computer science
SYNOPSIS Dihydrofolate reductase (E.C. 1.5.1.3) from Plasmodium falciparum and from its host, the owl monkey ( Aotus trivirgatus ). were partially purified and characterized. The molecular weight of the parasite enzyme was estimated to be over 10 times as high as that of the host enzyme. The host enzyme had 2 pH optima whereas the parasite enzyme only one. The activity of the host enzyme was greatly stimulated by KCI and urea, while that of the parasite enzyme was inhibited at high concentrations of such chaotropic agents. Km of the parasite enzyme was significantly higher than that of the host enzyme. The parasite enzyme had much lower K i for pyrimethamine than the host enzyme. Dihydrofolate reductases isolated from pyrimethamine‐resistant and pyrimethaminesensitive strains of P. falciparum were found to be similar.