Characterization of the plasma-membrane calcium pump from Trypanosoma cruzi
| Autor: | P J Romero, Felix A. Ruiz, Silvia N.J. Moreno, Gustavo Benaim, T Hermoso, G Hutchinson, W. De Souza, V Cervino, Roberto Docampo |
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| Rok vydání: | 1995 |
| Předmět: |
Erythrocytes
Calmodulin Swine Trypanosoma cruzi Calcium-Transporting ATPases Biology Biochemistry Chromatography Affinity Epitopes Affinity chromatography parasitic diseases Animals Humans Vanadate Molecular Biology chemistry.chemical_classification Antiserum Molecular mass Vesicle Cell Membrane Antibodies Monoclonal Cell Biology biology.organism_classification Molecular biology Microscopy Electron Enzyme chemistry biology.protein Cattle Research Article |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 0264-6021 |
| Popis: | Despite previous reports [McLaughlin (1985) Mol. Biochem. Parasitol. 15, 189-201; Ghosh, Ray, Sarkar and Bhaduri (1990) J. Biol. Chem. 265, 11345-11351; Mazumder, Mukherjee, Ghosh, Ray and Bhaduri (1992) J. Biol. Chem. 267, 18440-18446] suggesting that the plasma-membrane Ca(2+)-ATPases of different trypanosomatids differ from the Ca2+ pumps present in mammalian cells, Trypanosoma cruzi plasma-membrane Ca(2+)-ATPase shares several characteristics with the Ca2+ pumps present in other systems. This enzyme could be partially purified from epimastigote plasma-membrane vesicles using calmodulin-agarose affinity chromatography. The activity of the partially purified enzyme was stimulated by T. cruzi or bovine brain calmodulin. In addition, the enzyme cross-reacted with antiserum and monoclonal antibody 5F10 raised against human red-blood-cell Ca(2+)-ATPase, has a molecular mass of 140 kDa and forms Ca(2+)-dependent hydroxylamine-sensitive phosphorylated intermediates. These results, together with its high sensitivity to vanadate, indicate that this enzyme belongs to the P-type class of ionic pumps. |
| Databáze: | OpenAIRE |
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