Plasmodium berghei, P. chabaudi, and P. falciparum: similarities in phosphoproteins and protein kinase activities and their stage specific expression.
Phosphoproteins from Plasmodium berghei, P. chabaudi, and P. falciparum are compared. A major phosphoprotein of 46 kDa is found in all three species. Peptide mapping indicates that this protein is indeed the same in all three cases and is phosphorylated at similar sites in all three species. Monoclonal antibodies were raised against three other P. berghei phosphoproteins. All three monoclonal antibodies recognize both P. berghei and P. chabaudi proteins. Only one of the monoclonal antibodies crossreacts with a P. falciparum protein of 36 kDa, whereas the equivalent P. berghei and P. chabaudi proteins are 34 and 32 kDa, respectively. The highest rate of synthesis of the phosphoproteins is observed during the early trophozoite stage, whereas the highest rate of phosphorylation is observed during the late trophozoite stage.
Wiser
M F
MF
Max Planck Institut für Zellbiologie, Rosenhof, Ladenburg bei Heidelberg, Federal Republic of Germany.
Plitt
B
B
D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel; D004912:Erythrocytes / Q000469:parasitology; D008288:Malaria / Q000469:parasitology; D051379:Mice; D008970:Molecular Weight; D010750:Phosphoproteins / Q000302:isolation & purification / Q000378:metabolism*; D010766:Phosphorylation; D010961:Plasmodium / Q000201:enzymology* / Q000378:metabolism; D010962:Plasmodium berghei / Q000201:enzymology* / Q000378:metabolism; D010963:Plasmodium falciparum / Q000201:enzymology* / Q000378:metabolism; D011494:Protein Kinases / Q000302:isolation & purification / Q000378:metabolism*
D010750:Phosphoproteins; D011494:Protein Kinases