Partial purification and characterization of a murine malaria parasite, Plasmodium berghei specific aldolase.
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.
Kumar
S
S
Punjab Agricultural University, Ludhiana, India.
Banyal
H S
HS
D000818:Animals; D004305:Dose-Response Relationship, Drug; D004791:Enzyme Inhibitors / Q000494:pharmacology; D004912:Erythrocytes / Q000201:enzymology / Q000469:parasitology / Q000473:pathology; D005634:Fructose-Bisphosphate Aldolase / Q000302:isolation & purification* / Q000378:metabolism; D008288:Malaria / Q000378:metabolism / Q000469:parasitology / Q000662:veterinary; D051379:Mice; D018512:Parasitemia / Q000378:metabolism / Q000469:parasitology / Q000662:veterinary; D010962:Plasmodium berghei / Q000201:enzymology*
D004791:Enzyme Inhibitors; D005634:Fructose-Bisphosphate Aldolase