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Caracterización parcial de la calmodulina de Plasmodium falciparum

1995; National Institute of Health; Volume: 15; Issue: 4 Linguagem: Inglês

10.7705/biomedica.v15i4.880

2590-7379

Claudia P. Tinjacá, Moisés Wasserman,

Trypanosoma species research and implications

Partial purification of Plasmodium falciparum Calrnodulin (CaM) is described. Using highly specific monoclonal antibodies against CaM, we were able to separate two forms of this protein (a small form having a molecular weight of 12.600 anda bigger one of between 36.000 and 50.000 daltons), which separately are capable of stimulating the erythrocyte calcium ATPase. The possibility of a Plasmodium falciparum CaM structural modification, which does not interfere with its function as acalcium ATPase activator and makes it less sensible to CaM inhibitors than erythrocyte CaM, is proposed. Protein behaviour against CaM inhibitors, makes us believe that there is either an increase in calcium ATPase affinity ora modification of the inhibitors' interacting regulatory zone.