Cytosolic protein kinase activity associated with the maturation of the malaria parasite Plasmodium berghei.
Seven cytosolic phosphoproteins with relative molecular masses of 110, 58, 52, 46, 38, 36 and 34kDa and isoelectric points between 4.2 and 5.0 are identified from the rodent malaria parasite Plasmodium berghei. Similar patterns of phosphorylated proteins are obtained from parasite cytosol after incubation of intact infected erythrocytes with [32P]orthophosphate, or from parasite cytosol incubated with [gamma-32P]ATP. The characteristics of the phosphorylation reaction are similar to the previously described Plasmodium protein kinase [Wiser, M.F., Eaton, J.W. and Sheppard, J.R. (1983) J. Cell. Biochem. 21, 305-314], suggesting that the same protein kinase is involved. More protein phosphorylation activity is associated with the mature parasites than the immature forms, suggesting that these phosphoproteins may play some role in the parasite's erythrocytic stage cycle.
D000818:Animals; D003600:Cytosol / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel; D051379:Mice; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D010750:Phosphoproteins / Q000302:isolation & purification; D010766:Phosphorylation; D010962:Plasmodium berghei / Q000201:enzymology / Q000254:growth & development*; D011494:Protein Kinases / Q000378:metabolism*
D010446:Peptide Fragments; D010750:Phosphoproteins; D011494:Protein Kinases