NADP-specific isocitrate dehydrogenase from the simian malaria parasite Plasmodium knowlesi

partial purification and characterization.

Sanjeev Sahni, N. Saxena, S. K. Puri, G. P. Dutta, V. C. Pandey

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Cell-free schizonts of Plasmodium knowlesi, a simian malaria parasite, possess significant isocitrate dehydrogenase (IDH) activity, about 90% of which is contributed by the NADP-specific enzyme that is localized in the cytosolic fraction. The enzyme has been partially purified by affinity chromatography using Blue sepharose CL-6B. Although unstable in nature, it is stabilized by citrate and glycerol. Kinetic studies with DL-isocitrate and NADP yielded hyperbolic curves with Michaelis constants of 0.210 and 0.038 mM, respectively. Manganous or magnesium ions are essential for activity. The enzyme is thermosensitive, shows maximum activity at pH 8.0, and has a molecular mass of about 48.5 kDa. It is strongly inhibited by thiol-blocking agents but protected against them by thiol-providing agents. Cupric and argentic ions also have a marked inhibitory effect on its activity. The enzyme is significantly inhibited by chloroquine and oxytetracycline in vitro, but to a lesser degree by tetracycline.

Original languageEnglish (US)
Pages (from-to)338-342
Number of pages5
JournalJournal of Protozoology
Volume39
Issue number2
StatePublished - Mar 1992
Externally publishedYes

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Plasmodium knowlesi
Malaria
Parasites
Enzymes
NADP
Sulfhydryl Compounds
Ions
Schizonts
Isocitrate Dehydrogenase
Oxytetracycline
Chloroquine
Tetracycline
Affinity Chromatography
Citric Acid
Glycerol
Magnesium
isocitrate dehydrogenase (NADP+)

ASJC Scopus subject areas

  • Parasitology

Cite this

NADP-specific isocitrate dehydrogenase from the simian malaria parasite Plasmodium knowlesi : partial purification and characterization. / Sahni, Sanjeev; Saxena, N.; Puri, S. K.; Dutta, G. P.; Pandey, V. C.

In: Journal of Protozoology, Vol. 39, No. 2, 03.1992, p. 338-342.

Research output: Contribution to journalArticle

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