Key result
A soluble nitric oxide synthase from Leishmania donovani was purified and found to exist as a 230 kDa dimer with characteristics similar to mammalian NOS isoform I.
The study successfully isolated and characterized a nitric oxide synthase from Leishmania donovani, revealing similarities to mammalian NOS isoform I.
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Purified Leishmania NOS may guide studies on NO pathways in infection; leaves open its potential as a selective therapeutic target.
A soluble nitric oxide synthase (NOS) activity was purified 2800-fold from Leishmania donovani, the causative parasite of visceral leishmaniasis, by two-step affinity and anion-exchange chromatography. The purified enzyme ran as a prominent band of 110 kDa on SDS-PAGE whereas gel filtration experiments estimated the native molecular mass to be 230 +/- 20 kDa indicating that the native enzyme exists as a dimer. The enzyme activity required NADPH and was blocked by EGTA. The enzyme kinetics, cofactor requirements, inhibition studies and Western blot analysis with brain anti-NOS antibody suggest its similarity with mammalian NOS isoform I.
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Basu et al. (2006) studied Visceral leishmaniasis. Purification of nitric oxide synthase (NOS) was evaluated on Enzyme characteristics (molecular mass, kinetics, cofactor requirements). A soluble nitric oxide synthase from Leishmania donovani was purified and found to exist as a 230 kDa dimer with characteristics similar to mammalian NOS isoform I.
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