Protein kinase C in Trypanosoma cruzi epimastigote forms: partial purification and characterization
A protein kinase C activity from epimastigote forms of Trypanosoma cruzi was characterized. Cytosolic extracts were chromatographed on DEAE-cellulose columns giving two peaks of kinase activity which were eluted at 0.1 and 0.15 M NaCl. The first activity peak requires Ca2+ and phosphatidylserine for...
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| Otros Autores: | , , , |
| Formato: | Capítulo de libro |
| Lenguaje: | Inglés |
| Publicado: |
1989
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| Acceso en línea: | Registro en Scopus DOI Handle Registro en la Biblioteca Digital |
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| Sumario: | A protein kinase C activity from epimastigote forms of Trypanosoma cruzi was characterized. Cytosolic extracts were chromatographed on DEAE-cellulose columns giving two peaks of kinase activity which were eluted at 0.1 and 0.15 M NaCl. The first activity peak requires Ca2+ and phosphatidylserine for activity. Further kinase purification was performed by chromatography on phenyl Sepharose columns. In these columns the enzyme activity was adsorbed in the presence of Ca2+ and eluted with a EGTA-containing buffer. T. cruzi protein kinase C activity preferentially phosphorylated histone H1. It was stimulated by diacylglycerol and phorbol myristate acetate, and inhibited by polymyxin B and staurosporine. After subcellular fractionation of epimastigote cells, the kinase was found to be associated with microsomal and cytosolic fractions. © 1989. |
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| ISSN: | 01666851 |
| DOI: | 10.1016/0166-6851(89)90182-5 |