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1997•Journal of Veterinary Medicine Series BRequires access

Partial Purification and Characterization of a Murine Malaria Parasite, Plasmodium berghei Specific Aldolase

S. Kumar, H.S. Banyal

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Abstract

Cell-free P. berghei contains 26.1 times more aldolase activity as compared to normal mouse erythrocytes. Subcellular fractionation of cell-free parasite showed maximum enzyme activity in the soluble fraction. The parasite enzyme was active in a narrow pH range of 7.8-8.0. Of the enzyme activity 90% was lost within 2 weeks at 4 degrees C. Slight inhibition was observed with specific inhibitors ATP, pyrophosphate (PPi) and PEP. The F1, 6DP Km was 0.025 mM.

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What this paper is about

Cell-free P. berghei contains 26.1 times more aldolase activity as compared to normal mouse erythrocytes. Subcellular fractionation of cell-free parasite showed maximum enzyme activity in the soluble fraction. The parasite enzyme was active in a narrow pH range of 7.8-8.0. Of the enzyme activity 90% was lost within 2 weeks at 4 degrees C. Slight inhibition was observed with specific inhibitors ATP, pyrophosphate (PPi) and PEP. The F1, 6DP Km was 0.025 mM.

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Available abstract

Cell-free P. berghei contains 26.1 times more aldolase activity as compared to normal mouse erythrocytes. Subcellular fractionation of cell-free parasite showed maximum enzyme activity in the soluble fraction. The parasite enzyme was active in a narrow pH range of 7.8-8.0. Of the enzyme activity 90% was lost within 2 weeks at 4 degrees C. Slight inhibition was observed with specific inhibitors ATP, pyrophosphate (PPi) and PEP. The F1, 6DP Km was 0.025 mM.

Key concepts: Plasmodium berghei, Parasite hosting, Aldolase A, Enzyme, Biochemistry, Biology, Fractionation, Enzyme assay

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