Protein kinase C in Trypanosoma cruzi epimastigote forms: partial purification and characterization

GOMEZ, M.L.; ERIJMAN, L.; ARAUZO, S.; TORRES, H.N.; TELLEZ-IÑÓN, M.T.

MOLECULAR AND BIOCHEMICAL PARASITOLOGY

ELSEVIER SCIENCE BV

Lugar: San Antonio, TX; Año: 1989 vol. 36 p. 101 - 108

0166-6851

A protein kinase C activity from epimastigotc forms of Trypanosoma cruzi was characterized. Cvtosolic extracts were chromatographed on DEAE-ccllulose columns giving two peaks of kinase activity which were eluted at 0.1 and 0.15 M NaCl. The first activity peak requires Ca 2+ 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