Protein kinase C in Trypanosoma cruzi epimastigote forms: partial purification and characterization.
Mol Biochem Parasitol
; 36(2): 101-8, 1989 Sep.
Article
em En
| MEDLINE
| ID: mdl-2505073
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 and epimastigote cells, the kinase was found to be associated with microsomal and cytosolic fractions.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Trypanosoma cruzi
/
Proteína Quinase C
Limite:
Animals
Idioma:
En
Revista:
Mol Biochem Parasitol
Ano de publicação:
1989
Tipo de documento:
Article
País de afiliação:
Argentina
País de publicação:
Holanda