Purification and characterisation of the hexokinase of Plasmodium berghei, a murine malaria parasite.
Hexokinase (EC 2.7.1.1) activity in cell-free Plasmodium berghei was 35 and 5 times higher as compared to normal and P. berghei-infected mouse erythrocytes, respectively. Maximal enzyme activity was present in the cytosolic fraction of the isolated parasite. Manifold purification of parasite hexokinase was achieved with Sephadex G-200. Sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) revealed parasite enzyme subunit in the molecular weight range of 47 kDa with ATP (adenosine triphosphate) Km of 2 mM. Two out of three mice immunised with the hexokinase fraction were protected upon challenge with live parasites.
Kumar
S
S
Department of Immunology, College of Veterinary Science, Punjab Agricultural University, Ludhiana, India.
Banyal
H S
HS
D000255:Adenosine Triphosphate; D000818:Animals; D003600:Cytosol / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods / Q000662:veterinary; D004912:Erythrocytes / Q000469:parasitology*; D006593:Hexokinase / Q000032:analysis* / Q000302:isolation & purification*; D008288:Malaria / Q000097:blood / Q000662:veterinary; D051379:Mice / Q000097:blood / Q000469:parasitology*; D008970:Molecular Weight; D010962:Plasmodium berghei / Q000201:enzymology*; D012376:Rodent Diseases / Q000097:blood
D000255:Adenosine Triphosphate; D006593:Hexokinase